CFGparadigms - User contributions [en]

MediaWiki:Sidebar

2010-07-30T22:18:57Z

Heather Buschman:

MediaWiki:Sidebar

2010-07-30T22:18:10Z

Heather Buschman:

Instructions

2010-05-14T20:35:08Z

Heather Buschman:

Purpose: The purpose of the CFG Wiki paradigm pages is to involve Participating Investigators (PIs) in demonstrating how the CFG has made progress against its overall goal to 'define paradigms by which protein-carbohydrate interactions mediate cell communication.'
 
Process: The CFG's Paradigm Pages are open to contributions from all CFG Participating Investigators. To obtain editing privileges, you must first request an account and log in.
 
Focus: For consistency between paradigm pages, please maintain the 30 selected paradigm glycan-binding proteins (as seen on the Main Page) and the standard outline and formatting of each individual paradigm page as they appear. The CFG would be particularly grateful to PIs for filling in the gaps regarding:
 Progress toward understanding this GBP paradigm
 CFG resources used in investigations
 
'''How to edit the CFG Paradigm Pages:'''
* Click the 'Log in' link in the top right-hand corner
* Login or request a new account (enter any text in the 'biography' box) and wait for administrative approval. If you forgot your password, click 'E-mail new password'.
* From the [http://www.functionalglycomics.org/CFGparadigms Main Page], find the paradigm GBP you are interested in. Follow the link to that page.
* Click the 'edit' tab at the top of the page.
* You will see a text box containing all of the text and html tags that make up that paradigm page.
* Contribute 2-3 sentences for each of the blank fields (e.g. 'Progress toward understanding this GBP paradigm').
* If you can, contribute to the 'CFG resources used in investigations' section, including links to specific datasets in the [http://www.functionalglycomics.org CFG database].
* For formatting, use common html tags ([http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf see table]). ''Tip: Copy and paste text from the edit box of another Wiki page that contains the formatting style you would like to emulate.''
* Click 'Show preview' below the editing box.
* When finished, click 'Save page'.
* For more help editing Wiki pages, visit the [http://en.wikipedia.org/wiki/Help:Wiki_markup Wikipedia markup help page].

How to upload images

2010-05-13T21:03:37Z

Heather Buschman:

'''To upload a file or image to a wiki Paradigm Page:'''

<ol>
<li>From the 'toolbox’ on the left-hand menu of any of the CFG’s wiki Paradigm Pages, click ‘Upload file’ (You will need to login in order to see this link.)
<li>Follow the instructions to upload a file from your computer. Permitted file types include pdf, png, jpg, jpeg, gif, doc, xls, ppt. Make note of the ‘Destination filename’. 
''Example:'' File_name.jpg
<li>Go to the page where you want to upload an image. Click the ‘edit’ tab at the top.
<li>In the appropriate place in your editing box, insert an internal link to your image using the ‘Destination filename’ of the file you uploaded in Step 2. 
''Example:'' [[Image:Howtoupload3.png]]
<li>Click ‘Show preview’ at the bottom of the page and you should see your image.
<li>When satisfied, click 'Save page'.
</ol>
For more help uploading files, contact Anna at annacrie@scripps.edu.

File:Howtoupload3.png

2010-05-13T21:01:55Z

Heather Buschman:

Siglec-8

2010-05-13T18:59:52Z

Heather Buschman: /* Acknowledgements */

Siglec-8 is a human siglec expressed predominantly on eosinophils and mast cells, and is a paradigm for the rapidly evolving sub-family of CD33-related siglecs that are expressed on various white blood cells<ref>Crocker, P. R., Paulson, J. C. & Varki, A. Siglecs and their roles in the immune system. Nat Rev Immunol 7, 255-266 (2007).</ref><ref>Kikly, K.K., Bochner, B.S., et al. [http://www.ncbi.nlm.nih.gov/pubmed/10856141 Identification of SAF-2, a novel siglec expressed on eosinophils, mast cells, and basophils.] J Allergy Clin Immunol 105, 1093-100 (2000)</ref><ref name="Bochner 2009">Bochner, B.S. [http://www.ncbi.nlm.nih.gov/pubmed/19178537 Siglec-8 on human eosinophils and mast cells, and Siglec-F on murine eosinophils, are functionally related inhibitory receptors.] Clin Exp Allergy 39, 317-324 (2009).</ref><ref>Floyd, H. et al. Siglec-8. A novel eosinophil-specific member of the immunoglobulin superfamily. J Biol Chem 275, 861-866 (2000).</ref>. A characteristic feature of Siglec-8 and most other CD33-related siglecs is a cytoplasmic domain with a single immunoreceptor tyrosine inhibitory motif (ITIM) and a single ITIM-like motif that participate in siglec-mediated regulation of cell signaling and endocytosis. While there is no clear ortholog in mice, Siglec-F has been documented as a functional paralog that has a similar expression pattern on murine leukocytes and similar ligand specificity<ref name="Bochner 2009"/><ref>Tateno, H., Crocker, P. R. & Paulson, J. C. Mouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6'-sulfo-sialyl Lewis X as a preferred
glycan ligand. Glycobiology 15, 1125-1135 (2005).</ref><ref>Zhang, M. et al. Defining the in vivo function of Siglec-F, a CD33-related Siglec expressed on mouse
eosinophils. Blood 109, 4280-4287 (2007).</ref>. Siglec-8 and its paralog Siglec-F recognize a ligand containing both sialic acid and sulfate (NeuAcα2-3[6S]Galβ1-4G[Fucα1-3]GlcNAc-), a specificity that is distinct from all other siglecs. Ligation of Siglec-8 (or Siglec-F) with antibodies or polymeric ligands induces apoptosis of eosinophils, suggesting a therapeutic approach for treating eosinophil (or mast cell) mediated disease by targeting Siglec-8<ref>O'Reilly, M. K. & Paulson, J. C. Siglecs as targets for therapy in immune-cell-mediated disease. Trends Pharmacol Sci 30, 240-248 (2009).</ref><ref>Zimmermann, N. et al. Siglec-F antibody administration to mice selectively reduces blood and tissue
eosinophils. Allergy 63, 1156-1163 (2008).</ref><ref>Bochner, B. S. et al. Glycan array screening reveals a candidate ligand for Siglec-8. J Biol Chem 280, 4307-
4312 (2005).</ref><ref>Nutku, E., Aizawa, H., Hudson, S. A. & Bochner, B. S. Ligation of Siglec-8: a selective mechanism for induction of human eosinophil apoptosis. Blood 101, 5014-5020 (2003).</ref>.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
Participating Investigators (PIs) of the CFG have made major contributions to the understanding of the biology of Siglec-8 and its murine paralog, Siglec-F. These include: Bruce Bochner, Nicolai Bovin, Paul Crocker, James Paulson, Ronald Schnaar, Ajit Varki

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===
NeuAcα2-3(6-SO3)Galβ1-4(Fucα1-3)GlcNAc [6'Su-SLeX]

[[File:6pso3slex.jpg]]
 

=== Cellular expression ===
Human: Eosinophils, Mast Cells, Basophils
 

=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===
Eosinophil apoptosis
Inhibition of mast cell effector release
 

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Siglec-8&maxresults=20 CFG database search results for Siglec-8].

=== Glycan profiling ===
Glycan structure analysis has been conducted by the CFG for human and mouse eosinophils.

=== Glycogene microarray ===
Analysis has been conducted on glycosyltransferase expression using the glycogene microarray for murine eosinophils.

=== Knockout mouse lines ===

 
=== Glycan array ===
The discovery of the ligand for siglec-8 and its murine paralog, Siglec-F, was made by investigator-initiated resource requests for glycan array analysis and carbohydrate compounds.

== Related GBPs ==
hSiglec-3 (CD33), Siglec-5, Siglec-6, Siglec, 7, Siglec-9, Siglec-10, Siglec-11, Siglec-F, Siglec-E, Siglec-G

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Bruce Bochner, Paul Crocker, James Paulson, Ron Schnaar

Quick guide to formatting

2010-05-13T18:58:10Z

Heather Buschman: Created page with 'For quick reference while editing these wiki pages, download this PDF to your computer: [http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf guide to wik…'

For quick reference while editing these wiki pages, download this PDF to your computer: [http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf guide to wiki formatting].

MediaWiki:Sidebar

2010-05-13T18:57:14Z

Heather Buschman:

How to upload images

2010-05-13T18:56:21Z

Heather Buschman:

'''To upload a file or image to a wiki Paradigm Page:'''

<ol>
<li>From the 'toolbox’ on the left-hand menu of any of the CFG’s wiki Paradigm Pages, click ‘Upload file’ (You will need to login in order to see this link.)
<li>Follow the instructions to upload a file from your computer. Permitted file types include pdf, png, jpg, jpeg, gif, doc, xls, ppt. Make note of the ‘Destination filename’. 
''Example:'' File_name.jpg
<li>Go to the page where you want to upload an image. Click the ‘edit’ tab at the top.
<li>In the appropriate place in your editing box, insert an internal link to your image using the ‘Destination filename’ of the file you uploaded in Step 2. 
''Example:'' Type: Image:File_name.jpg and add double brackets on either side: [[ ]]
<li>Click ‘Show preview’ at the bottom of the page and you should see your image.
<li>When satisfied, click 'Save page'.
</ol>
For more help uploading files, contact Anna at annacrie@scripps.edu.

How to upload images

2010-05-13T18:53:32Z

Heather Buschman: Created page with ''''To upload a file or image to a wiki Paradigm Page:''' <ol> <li>From the 'toolbox’ on the left-hand menu of any of the CFG’s wiki Paradigm Pages, click ‘Upload file’ (…'

'''To upload a file or image to a wiki Paradigm Page:'''

<ol>
<li>From the 'toolbox’ on the left-hand menu of any of the CFG’s wiki Paradigm Pages, click ‘Upload file’ (You will need to login in order to see this link.)
<li>Follow the instructions to upload a file from your computer. Permitted file types include pdf, png, jpg, jpeg, gif, doc, xls, ppt. Make note of the ‘Destination filename’. 
''Example:'' Galectin_18.jpg
<li>Go to the page where you want to upload an image. Click the ‘edit’ tab at the top.
<li>In the appropriate place in your editing box, insert an internal link to your image using the ‘Destination filename’ of the file you uploaded in Step 2. 
''Example:'' Type 'Image:Galectin_18.jpg' and add double brackets on either side: [[ ]]
<li>Click ‘Show preview’ at the bottom of the page and you should see your image.
<li>When satisfied, click 'Save page'.
</ol>
For more help uploading files, contact Anna at annacrie@scripps.edu.

Help:Editing

2010-05-13T18:45:56Z

Heather Buschman: Created page with ''''How to edit the CFG Paradigm Pages:''' * Click the 'Log in' link in the top right-hand corner * Login or request a new account (enter any text in the 'biography' box) and wait…'

'''How to edit the CFG Paradigm Pages:'''
* Click the 'Log in' link in the top right-hand corner
* Login or request a new account (enter any text in the 'biography' box) and wait for administrative approval. If you forgot your password, click 'E-mail new password'.
* From the [http://www.functionalglycomics.org/CFGparadigms Main Page], find the paradigm GBP you are interested in. Follow the link to that page.
* Click the 'edit' tab at the top of the page.
* You will see a text box containing all of the text and html tags that make up that paradigm page.
* Contribute 2-3 sentences for each of the blank fields (e.g. 'Progress toward understanding this GBP paradigm').
* If you can, contribute to the 'CFG resources used in investigations' section, including links to specific datasets in the [http://www.functionalglycomics.org CFG database].
* For formatting, use common html tags ([http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf see table]). ''Tip: Copy and paste text from the edit box of another Wiki page that contains the formatting style you would like to emulate.''
* Click 'Show preview' below the editing box.
* When finished, click 'Save page'.
* For more help editing Wiki pages, visit the [http://en.wikipedia.org/wiki/Help:Wiki_markup Wikipedia markup help page].

MediaWiki:Sidebar

2010-05-13T18:41:09Z

Heather Buschman:

Instructions

2010-05-13T18:16:09Z

Heather Buschman:

Purpose: The purpose of the CFG Wiki paradigm pages is to involve Participating Investigators (PIs) in demonstrating how the CFG has made progress against its overall goal to 'define paradigms by which protein-carbohydrate interactions mediate cell communication.'
 
Process: The CFG is currently working with 1-2 experts per page as they begin filling in the wiki Paradigm Pages. To obtain editing privileges, you must 'login'.
 
Focus: For consistency between paradigm pages, please maintain the 30 selected paradigm glycan-binding proteins (as seen on the Main Page) and the standard outline and formatting of each individual paradigm page as they appear. The CFG would be particularly grateful to PIs for filling in the gaps regarding:
 Progress toward understanding this GBP paradigm
 CFG resources used in investigations
 
'''How to edit the CFG Paradigm Pages:'''
* Click the 'Log in' link in the top right-hand corner
* Login or request a new account (enter any text in the 'biography' box) and wait for administrative approval. If you forgot your password, click 'E-mail new password'.
* From the [http://www.functionalglycomics.org/CFGparadigms Main Page], find the paradigm GBP you are interested in. Follow the link to that page.
* Click the 'edit' tab at the top of the page.
* You will see a text box containing all of the text and html tags that make up that paradigm page.
* Contribute 2-3 sentences for each of the blank fields (e.g. 'Progress toward understanding this GBP paradigm').
* If you can, contribute to the 'CFG resources used in investigations' section, including links to specific datasets in the [http://www.functionalglycomics.org CFG database].
* For formatting, use common html tags ([http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf see table]). ''Tip: Copy and paste text from the edit box of another Wiki page that contains the formatting style you would like to emulate.''
* Click 'Show preview' below the editing box.
* When finished, click 'Save page'.
* For more help editing Wiki pages, visit the [http://en.wikipedia.org/wiki/Help:Wiki_markup Wikipedia markup help page].

More help

2010-05-13T18:11:03Z

Heather Buschman: Blanked the page

Quick guide to editing

2010-05-13T18:09:57Z

Heather Buschman:

For quick reference while editing these wiki pages, download this PDF to your computer: [http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf guide to wiki formatting].

P-Selectin

2010-05-13T18:05:59Z

Heather Buschman: /* Acknowledgements */

The three selectins (P-selectin, L-selectin, and E-selectin) have related and sometimes overlapping functions in cell adhesion and mediate some of the best characterized glycan-dependent cell adhesion events. Of these three C-type lectins, the target ligand of P-selectin, P-selectin glycoprotein ligand 1 (PSGL-1), is the best understood. Thus, P-selectin is used here to represent all three selectins.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
Selectin research was already at a relatively mature stage when the CFG began. Early PI work included structural studies, extensive analysis of leukocyte adhesion to endothelia ''in vivo'', and characterization of knockout mice to demonstrate physiological function. In addition to submitting samples for glycan array analysis, PIs have been involved in analyzing selectin expression under different conditions, including in knockout mice lacking enzymes for making target ligands.
* PIs working on P-selectin include: Hans-Peter Altevogt, Bruce Bochner, Pi-Wan Cheng, Richard Cummings, Robert Fuhlbrigge, Minoru Fukuda, Geoff Kansas, Klaus Ley, John Lowe, Rodger McEver, Steve Rosen, Ron Schnaar, Karen Snapp, Lloyd Stoolman, Martin Wild, Hermann Ziltener
* Non-PIs who have used CFG resources to study P-selectin include: Roland Contreras, Leonard Seymour

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=P-selectin&maxresults=20 CFG database search results for P-selectin].

=== Glycan profiling ===
The glycans on the main target for P-selectin, P-selectin glycoprotein ligand 1 (PSGL-1), were analyzed.

=== Glycogene microarray ===
Regulation of P-selectin expression was analyzed under multiple conditions.

=== Knockout mouse lines ===
The [https://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of PSGL-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
The comparative binding specificities of human and mouse selectins were analyzed.

== Related GBPs ==
L-selectin and E-selectin

== References ==
<references/>
* Mitoma J, Miyazaki T, Sutton-Smith M, Suzuki M, Saito H, Yeh JC, Kawano T, Hindsgaul O, Seeberger PH, Panico M, Haslam SM, Morris HR, Cummings RD, Dell A, Fukuda M (2009) The N-glycolyl form of mouse sialyl Lewis X is recognized by selectins but not by HECA-452 and FH6 antibodies that were raised against human cells. Glycoconj J 26, 511-523.
* Kawar ZS, Johnson TK, Natunen S, Lowe JB, Cummings RD (2008) PSGL-1 from the murine leukocytic cell line WEHI-3 is enriched for core 2-based O-glycans with sialyl Lewis x antigen. Glycobiology 18, 441-446.
* Mitoma J, Bao X, Petryanik B, Schaerli P, Gauguet JM, Yu SY, Kawashima H, Saito H, Ohtsubo K, Marth JD, Khoo KH, von Andrian UH, Lowe JB, Fukuda M (2007) Critical functions of N-glycans in L-selectin-mediated lymphocyte homing and recruitment. Nat Immunol 8, 409-418.
* Veerman KM, Williams MJ, Uchimura K, Singer MS, Merzaban JS, Naus S, Carlow DA, Owen P, Rivera-Nieves J, Rosen SD, Ziltener HJ (2007) Interaction of the selectin ligand PSGL-1 with chemokines CCL21 and CCL19 facilitates efficient homing of T cells to secondary lymphoid organs. Nat Immunol 8, 532-539.
* Chen S, Kawashima H, Lowe JB, Lanier LL, Fukuda M (2005) Suppression of tumor formation in lymph nodes by L-selectin-mediated natural killer cell recruitment. J Exp Med 202, 1679-1689.
* Kawashima H, Petryniak B, Hiraoka N, Mitoma J, Huckaby V, Nakayama J, Uchimura K, Kadomatsu K, Muramatsu T, Lowe JB, Fukuda M (2005) N-acetylglucosamine-6-O-sulfotransferases 1 and 2 cooperatively control lymphocyte homing through L-selectin ligand biosynthesis in high endothelial venules. Nat Immunol 6, 1096-1104.
* Piccio L, Rossi B, Colantonio L, Grenningloh R, Gho A, Ottoboni L, Homeister JW, Scarpini E, Martinello M, Laudanna C, DAmbrosio D, Lowe JB, (2005) Constantin G Efficient recruitment of lymphocytes in inflamed brain venules requires expression of cutaneous lymphocyte antigen and fucosyltransferase-VII. J Immunol 174, 5805-5813.
* Homeister JW, Daugherty A, Lowe JB (2004) α(1,3)Fucosyltransferases FucT-IV and FucT-VII control susceptibility to atherosclerosis in apolipoprotein E -/- mice. Arterioscler Thromb Vasc Biol 24, 1897-1903.
* Lowe JB (2003) Glycan-dependent leukocyte adhesion and recruitment in inflammation Curr Opin Cell Biol 15, 531-538.
* Smith PL, Myers JT, Rogers CE, Zhou L, Petryniak B, Becher DJ, Homeister JW, Lowe JB (2002) Conditional control of selectin ligand expression and global fucosylation events in mice with a targeted mutation at the FX locus. J Cell Biol 158, 801-815.

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Minoru Fukuda, Yvette van Kooyk

Galectin-3

2010-05-13T18:05:34Z

Heather Buschman: /* Acknowledgements */

Galectin-3...
* is the only member of chimeric subfamily in mammals
* is a very well-studied glycan-binding protein (GBP)
* crystal structure is known
* has unique functions intra- and extra-cellularly, due to unusual N-terminal domain that can participate in protein-protein interactions
* has a unique mode of multimerization
* is the only known anti-apoptotic galectin
* null mice have distinct phenotypes, including alterations in inflammatory and wound-healing responses, and cyst formation in disease<ref>Chiu, M.G. et al. Galectin-3 associates with the primary cilium and modulates cyst growth in congenital polycystic kidney disease. Am J Pathol 169, 1925-1938 (2006).</ref>
* has unique functions in innate immune response to microbial pathogens
* has been administered in animal models of disease to assess therapeutic potential
* binds distinct cell surface glycoprotein ligands in lymphocytes compared to Galectin-16
* expression is involved in growth modulation<ref>Baptiste, T.A., James, A., Saria, M. & Ochieng, J. Mechano-transduction mediated secretion and uptake of
Galectin-3 in breast carcinoma cells: implications in the extracellular functions of the lectin. Exp Cell Res 313, 652-664 (2007). </ref>
* has anti-apoptotic activity in its intracellular expression<ref>Saegusa, J. et al. Galectin-3 protects keratinocytes from UVB-induced apoptosis by enhancing AKT activation and suppressing ERK activation. J Invest Dermatol 128, 2403-2411 (2008).</ref>

== CFG Participating Investigators contributing to the understanding of this paradigm ==
CFG Participating Investigators (PIs) contributing to the understanding of Galectin-3 include: Linda Baum, Susan Bellis, Roger Chammas, Richard Cummings, James Dennis, Margaret, Huflejt, Fu-Tong Liu, Joshiah Ochieng, Noorjahan Panjawani, Mauro Perretti, Avram Raz, James Rini, Maria Roque-Barreira, Sachiko Sato, Tariq Sethi, Irma van Die, Gerardo Vasta, John Wang, Paul Winyard

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-3&maxresults=20 CFG database search results for Galectin-3].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
Galectin-3 knockout mice were [https://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotyped] by the CFG and continue to be used by investigators to study the biological functions of Galectin-3.

=== Glycan array ===
Investigators have used CFG carbohydrate compounds and glycan array to study ligand binding specificity of Galectin-3.

== Related GBPs ==
None in mammals, homologues in invertebrates.

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Michael Demetriou, Fu-Tong Liu

Siglec-15

2010-05-13T18:04:43Z

Heather Buschman: /* Acknowledgements */

Siglec-15 serves as a paradigm for several siglecs, including Siglec-14<ref>Angata, T., Hayakawa, T., Yamanaka, M., Varki, A. & Nakamura, M. Discovery of Siglec-14, a novel sialic acid receptor undergoing concerted evolution with Siglec-5 in primates. Faseb J 20, 1964-1973 (2006).</ref>, Siglec-16<ref>Cao, H. et al. SIGLEC16 encodes a DAP12-associated receptor expressed in macrophages that evolved from its inhibitory counterpart SIGLEC11 and has functional and non-functional alleles in humans. Eur J Immunol 38, 2303-2315 (2008).</ref> and Siglec-H<ref>Zhang, J. et al. Characterization of Siglec-H as a novel endocytic receptor expressed on murine plasmacytoid dendritic cell precursors. Blood 107, 3600-3608 (2006).</ref><ref>Blasius, A. L., Cella, M., Maldonado, J., Takai, T. & Colonna, M. Siglec-H is an IPC-specific receptor that modulates type I IFN secretion through DAP12. Blood 107, 2474-2476 (2006).</ref>, that contain a basic amino acid within the transmembrane domain<ref>Delputte, P. L. et al. Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic81, 9546-9550 (2007).</ref>. This leads to association of these siglecs with a transmembrane adaptor protein containing an immunoreceptor tyrosine based activation motif (ITAM). Siglec-15 is unusual compared to other siglecs that share this paradigm in two respects. Firstly it can associate with two ITAM containing adaptors, DAP12 and DAP10, whereas Siglec-14, Siglec-16, and Siglec-H show a restricted association with DAP12. Siglec-15 is also unusual in having four cysteine residues in the V-set domain predicted to result in an inter-sheet disulfide that is absent from all other known siglecs. These potentially ‘activating’ siglecs are expressed on myeloid cells and dendritic cells and may be involved in innate responses to pathogen challenge.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
As yet, no CFG Participating Investigators (PIs) have contributed to Siglec-15, but contributors to the related Siglec-H include Marco Colonna and Paul Crocker.

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Siglec-15&maxresults=20 CFG database search results for Siglec-15].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
The CFG has generated Siglec-15-deficient ES cells that will permit generation of a Siglec-15-deficient mouse in the future. Two [https://www.functionalglycomics.org/static/consortium/resources/DataCoreFsigH.shtml Siglec-H-deficient mouse lines] (Siglec-H-conditional knockout and Siglec-H-total knockout) were also generated and are currently under investigation.

=== Glycan array ===

== Related GBPs ==
Siglec-14, Siglec-16, Siglec-H

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Takashi Angata, Paul Crocker, James Paulson

Reovirus hemagglutinin (sigma 1)

2010-05-13T18:03:50Z

Heather Buschman: /* Acknowledgements */

'''Mammalian orthoreoviruses (reoviruses)''' are useful models for studies of viral receptor recognition and the pathogenesis of viral disease. Reovirus also efficiently lyses tumor cells in experimental animals<ref>Duncan, M.R., Stanish, S.M., and Cox, D.C. Differential sensitivity of normal and transformed human cells to reovirus infection. J. Virol. 28:444-449, 1978.</ref><ref> Coffey, M.C., Strong, J.E., Forsyth, P.A., and Lee, P.W. Reovirus therapy of tumors with activated Ras pathway. Science 282:1332-1334, 1998.</ref> and has shown efficacy in clinical trials for aggressive and refractory human tumors<ref>Stoeckel, J., and Hay, J.G. Drug evaluation: Reolysin--wild-type reovirus as a cancer therapeutic. Curr. Opin. Mol. Ther. 8:249-260, 2006.</ref><ref>Twigger, K., Vidal, L., White, C.L., De Bono, J.S., Bhide, S., Coffey, M., Thompson, B., Vile, R.G., Heinemann, L., Pandha, H.S., et al. Enhanced in vitro and in vivo cytotoxicity of combined reovirus and radiotherapy. Clin. Cancer Res. 14:912-923, 2008. </ref>. Reovirus forms double-shelled particles<ref>Dryden, K.A., Wang, G., Yeager, M., Nibert, M.L., Coombs, K.M., Furlong, D.B., Fields, B.N., and Baker, T.S. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1023-1041, 1993.</ref> that contain a segmented dsRNA genome. The reovirus sigma 1 protein is a long, fiber-like molecule that extends from the virion surface<ref>Furlong, D.B., Nibert, M.L., and Fields, B.N. Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles. J. Virol. 62:246-256, 1988.</ref> and mediates viral attachment<ref>Weiner, H.L., Ault, K.A., and Fields, B.N. Interaction of reovirus with cell surface receptors. I. Murine and human lymphocytes have a receptor for the hemagglutinin of reovirus type 3. J. Immunol. 124:2143-2148, 1980.</ref><ref>Lee, P.W.K., Hayes, E.C., and Joklik, W.K. Protein σ1 is the reovirus cell attachment protein. Virology 108:156-163, 1981.</ref>. The three human serotypes (T1, T2, and T3) differ in cellular tropism, which correlates directly with receptor-binding properties of sigma 1. Sialic acid serves as an essential receptor for T3 reovirus on murine erythroleukemia (MEL) cells<ref>Rubin, D.H., Wetzel, J.D., Williams, W.V., Cohen, J.A., Dworkin, C., and Dermody, T.S. Binding of type 3 reovirus by a domain of the σ1 protein important for hemagglutination leads to infection of murine erythroleukemia cells. J. Clin. Invest. 90:2536-2542, 1992.</ref>, and it functions as a coreceptor on murine L929 (L) cells<ref>Gentsch, J.R., and Pacitti, A.F. Effect of neuraminidase treatment of cells and effect of soluble glycoproteins on type 3 reovirus attachment to murine L cells. J. Virol. 56:356-364, 1985.</ref><ref>Pacitti, A., and Gentsch, J.R. Inhibition of reovirus type 3 binding to host cells by sialylated glycoproteins is mediated through the viral attachment protein. J. Virol. 61:1407-1415, 1987. </ref><ref>Paul, R.W., Choi, A.H., and Lee, P.W.K. The α-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus. Virology 172:382-385, 1989.</ref><ref>Rubin, D.H., Wetzel, J.D., Williams, W.V., Cohen, J.A., Dworkin, C., and Dermody, T.S. Binding of type 3 reovirus by a domain of the σ1 protein important for hemagglutimurine erythroleukemia cells. J. Clin. Invest. 90:2536-2542, 1992.</ref><ref>Nibert, M.L., Chappell, J.D., and Dermody, T.S. Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved σ1 protein. J. Virol. 69:5057-5067, 1995.</ref>. Residues involved in sialic acid-binding map to the center of the long fiber, close to the midpoint of the molecule<ref>Chappell, J.D., Prota, A., Dermody, T.S., and Stehle, T. Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 21:1-11, 2002.</ref>, in a repetitive structural region known as the triple β-spiral. The T1 sigma 1 protein binds to cell-surface glycans of unknown structure.

The triple β-spiral of '''sigma 1''' functions as a trimerization domain and defines a novel carbohydrate-recognition motif. Other carbohydrate-recognition domains, such as those of the C-type lectin superfamily<ref>Weis, W.I., Taylor, M.E., and Drickamer, K. The C-type lectin superfamily in the immune system. Immunol. Rev. 163:19-34, 1998.</ref> or the sialic acid-binding domains in the Siglec family of adhesion proteins<ref>Crocker, P.R., and Varki, A. Siglecs in the immune system. Immunology 103:137-145, 2001.</ref>(see [http://glycobank.mit.edu/glycoWiki/Main_Page Siglec paradigms]), have been described, but none are formed by a repetitive, fiber-like structure such as the one present in sigma 1. In fact, the domain in sigma 1 that binds sialic acid constitutes a carbohydrate-binding “cassette” that could be endowed with altered ligand-binding properties or grafted onto other trimeric structures and used to create avidity for carbohydrates. For example, the adenovirus fiber shaft could be licensed with sialic acid-binding capacity using this approach. These properties render the sigma 1 protein unique among the structurally known glycan-binding moieties.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
CFG Participating Investigators (PIs) contributing to the understanding of sigma 1 include: Terence Dermody, Thilo Stehle

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=reovirus&maxresults=20 CFG database search results for "reovirus"].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

 
=== Glycan array ===

 
== Related GBPs ==
The attachment protein of adenovirus, fiber, is a structural homolog of sigma 1. At least one adenovirus serotype (Ad37) is known to bind glycan receptors via residues in the fiber protein<ref>Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N: Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. Journal of Virology 2004, 78:7727-7736.</ref>. The actual binding site is not homologous. However, information about reovirus glycan binding could also be used to engineer adenovirus fiber proteins (or other trimeric fiber-like proteins) that possess novel glycan-binding properties.

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Terence Dermody, Mavis McKenna, Thilo Stehle

Candida glabrata EPA7

2010-05-13T17:59:13Z

Heather Buschman: /* Acknowledgements */

'''Fungal adhesins with lectin properties''' 
Cell adhesion proteins on fungal cell surfaces mediate interactions both with other cells of the same type and with the external environment<ref>Douglas, L.M., Li, L., Yang, Y. and Dranginis, A.M. 2007. Expression and characterization of the flocculin Flo11/Muc1, a Saccharomyces cerevisiae mannoprotein with homotypic properties of adhesion. Eukaryot Cell, 6, 2214-2221.</ref><ref>Dranginis, A.M., Rauceo, J.M., Coronado, J.E. and Lipke, P.N. 2007. A biochemical guide to yeast adhesins: glycoproteins for social and antisocial occasions. Microbiol Mol Biol Rev, 71, 282-294.</ref>. These interactions impact critical processes including mating, pathogenesis, and biofilm formation. Fungal adhesins are typically GPI-anchored proteins that have been covalently liked to the cell wall, such that their N-terminal ligand binding domains extend from the cell surface. They frequently occur as families of related proteins<ref>Tronchin, G., Pihet, M., Lopes-Bezerra, L.M. and Bouchara, J.P. 2008. Adherence mechanisms in human pathogenic fungi. Med Mycol, 46, 749-772. </ref>. Members of two such groups, the flocculation/agglutination genes of the model yeast ''Saccharomyces cerevisiae''<ref>Kobayashi, O., Hayashi, N., Kuroki, R. and Sone, H. 1998. Region of FLO1 proteins responsible for sugar recognition. J Bacteriol, 180, 6503-6510.</ref> and the related EPA genes<ref>Kaur, R., Domergue, R., Zupancic, M.L. and Cormack, B.P. 2005. A yeast by any other name: Candida glabrata and its interaction with the host. Curr Opin Microbiol, 8, 378-384.</ref> of the pathogenic fungus ''Candida glabrata'', are lectins. Several of the 23 identified EPA genes have been functionally shown to mediate binding of ''C. glabrata'' to host cells<ref name="Castano 2005">Castano, I., Pan, S.J., Zupancic, M., Hennequin, C., Dujon, B. and Cormack, B.P. 2005. Telomere length control and transcriptional regulation of subtelomeric adhesins in Candida glabrata. Mol Microbiol, 55, 1246-1258.</ref><ref>Domergue, R., Castano, I., de las Penas, A., Zupancic, M., Lockatell, V., Hebel, J.R. et al. 2005. Nicotinic acid limiation regulates silencing of Candida albicans adhesins during UTI. Science, 308, 866-870.</ref>, an essential step in infection and virulence. Defining the specificity of these proteins and their biological roles will elucidate the interactions between host and pathogen, and potentially indicate ways in which to inhibit them for the benefit of the host.

'''''Candida glabrata'' EPA7''' 
The EPA family was chosen as a paradigm because of its relevance to a fungal pathogen that affects human health, and which also can be studied in mouse models of infection. EPA7 was chosen to represent this group because it has been demonstrated to function as an adhesin<ref name="Castano 2005"/> and is one of the EPA proteins that has been studied in the most detail. The N-terminal binding domain of this protein, expressed on the surface of S''. cerevisiae'', has been analyzed on the CFG glycan array. These studies demonstrated EPA7 binding specificity for β1,3- and β1,4-linked galactosides<ref>Zupancic, M.L., Frieman, M., Smith, D., Alvarez, R.A., Cummings, R.D. and Cormack, B.P. 2008. Glycan microarray analysis of Candida glabrata adhesin ligand specificity. Mol Microbiol, 58, 547-559.</ref><ref>de Groot, P.W.J. and Klis, F.M. 2008. The conserved PA14 domain of cell wall-associated fungal adhesins governs their glycan-binding specificity. Mol Microbiol, 68, 535-537. </ref>. This work represents a significant step forward in the area of lectin-like fungal adhesins; in general the specificity of these important proteins remains unexplored.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
* CFG Participating Investigators (PIs) who have contributed to studies of this paradigmatic protein include: Brendan Cormack, Rick Cummings
* PIs using CFG resources to study related ''S. cerevisiae'' proteins include: Lars-Oliver Essen (several flocculins), Peter Lipke (alpha agglutinin)

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=EPA7&maxresults=20 CFG database search results for "EPA7"].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

 
=== Glycan array ===
The specificity of EPA7 and related proteins was determined through CFG glycan array analysis.

== Related GBPs ==
* 22 additional EPA family members in ''C. glabrata''
* Related proteins in ''S. cerevisiae''
* EPA7-like glycan-binding domain also occurs in predicted proteins of ''Ashbya gossypii'' and ''Kluyveromyces lactis''.

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Richard Cummings, Tamara Doering, Peter Lipke

DC-SIGN

2010-05-13T17:58:50Z

Heather Buschman: /* Acknowledgements */

DC-SIGN is a C-type lectin that plays roles in both cell-cell and host-pathogen interactions, and thus serves as a model for both processes. This glycan-binding protein (GBP) paradigm also serves as a model for other members of the C-type lectin family expressed on dendritic cells.

== CFG Participating Investigators contributing to the understanding of this paradigm ==

Many investigators, both CFG Participating Investigators (PIs) and non-PIs using CFG resources, have led extensive studies on DC-SIGN, particularly regarding structure-function relationships, interactions with pathogens, and signaling functions in dendritic cells.
* PIs working on DC-SIGN include: Pedro Bonay, Angel Corbi, Kurt Drickamer, Juan Garcia-Vallejo, Donald Harn, Kayo Inaba, Benhur Lee, Olivier Neyrolles, Irma van Die, Yvette van Kooyk, William Weis, Martin Wild
* Non-PIs who have used CFG resources to study DC-SIGN include: Brigitte Gicquel, Arne Skerra, Ralph Steinman

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=DC-SIGN&maxresults=20 CFG database search results for DC-SIGN].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

Knockout mice for three potential DC-SIGN orthologues ([https://www.functionalglycomics.org/static/consortium/resources/DataCoreFdc.shtml DC-SIGN], [https://www.functionalglycomics.org/static/consortium/resources/DataCoreFsr1.shtml SIGNR1], and [https://www.functionalglycomics.org/static/consortium/resources/DataCoreFsr3.shtml SIGNR3]) were created by the CFG and distributed to PIs, and their [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotypes] were analyzed.

=== Glycan array ===

Glycan array analysis and synthetic oligosaccharides were used to elucidate DC-SIGN glycan-binding specificity and analyze the mechanism of specific glycan binding.

== Related GBPs ==
Other dendritic cell lectins include langerin, DCIR, and DCAR. Paralogs on other cells include DC-SIGNR.

== References ==
<references/>
* Tanne A, Ma B, Boudou F, Tailleux L, Botella H, Badell E, Levillain F, Taylor ME, Drickamer K, Nigou J, Dobos KM, Puzo G, Vestweber D, Wild MK, Marcinko M, Sobieszczuk P, Stewart L, Lebus D, Gicquel B, Neyrolles O (2009) A murine DC-SIGN homologue contributes to early host defense against Mycobacterium tuberculosis. J Exp Med 206, 2205-2220.
* Powlesland AS, Ward EM, Sadhu SK, Guo Y, Taylor ME, Drickamer K (2006) Novel mouse homologs of human DC-SIGN: Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins. J Biol Chem 281, 20440-20449.
* Van Liempt E, Bank CM, Mehta P, Garci A-Vallejo JJ, Kawar ZS, Geyer R, Alvarez RA, Cummings RD, van Kooyk Y, van Die I (2006) Specificity of DC-SIGN for mannose- and fucose-containing glycans. FEBS Lett 580, 6123-6131.
* Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, Taylor ME, Weis WI, Drickamer K (2004) Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nat Struct Mol Biol 11, 591-598.

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Irma van Die, Yvette van Kooyk

Ficolins/Mannose-binding protein

2010-05-13T17:58:13Z

Heather Buschman: /* Acknowledgements */

The ficolins share a common organization and function with the collectins: serum mannose-binding and the pulmonary surfactant proteins C and D. All of these proteins are soluble mediators of innate immunity and consist of globular sugar-binding domains attached to collagenous stalks, which can invoke innate immune responses either through complement fixation or interaction with receptors on the surfaces of macrophages. Amongst these proteins, the ficolins have been most extensively investigated with CFG resources, while mannose-binding protein is the best characterized. The ficolins have fibrinogen-like sugar-binding domains, rather than C-type carbohydrate-recognition domains, but conceptually fall within the same group.

See also: paradigm page for [[Ficolin M (Ficolin 1)]]
== CFG Participating Investigators contributing to the understanding of this paradigm ==
Participating Investigators have generated and characterized knockout mice, defined the sugar-binding properties and undertaken structural analysis for members of this glycan-binding protein (GBP) group.
* PIs working on ficolins include: Raymond Dwek, Daniel Mitchell, Nicole Thielens
* PIs investigating other paradigms in this GBP group include: Kurt Drickamer, Ten Feizi, Toshisuke Kawasaki, Laura Kiessling, Reiko Lee, Yuan Lee, Jamie Marth, Kenneth Ng, Michel Nussenzweig, Pauline Rudd, Maureen Taylor, Bill Weis
* Non-PIs with who have used CFG resources to study ficolins include: David Stephens

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=ficolin&maxresults=20 ficolin] and [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=mannose-binding&maxresults=20 mannose-binding receptor].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

 
=== Glycan array ===
The binding specificities of several of the ficolins have been analyzed and other members of the group were screened on the CFG glycan array.

== Related GBPs ==
Serum mannose-binding protein (MBP, also designated mannose-binding lectin, MBL) and the pulmonary surfactant proteins SP-C and SP-D

== References ==
<references/>
* Gout E, Garlatti V, Smith DF, Lacroix M M, Dumestre-Perard C, Lunardi T, Martin L, Cesbron JY, Arlaud GJ, Gaboriaud C, Thielens NM (2010) Carbohydrate recognition properties of human ficolins: Glycan array screening reveals the sialic acid binding specificity of M-ficolin. J Biol Chem 285, 6612-6622.
* Krarup A, Mitchell DA, Sim RB (2008) Recognition of acetylated oligosaccharides by human L-ficolin. Immunol Lett 118, 152-6.

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Nicole Thielens, Daniel Mitchell, Yvette van Kooyk

Galectin-1

2010-05-13T17:57:41Z

Heather Buschman: /* Acknowledgements */

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte development and increased susceptibility to autoimmune disease.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential.
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings, Gabriel Rabinovich

Siglec-8

2010-05-13T17:57:02Z

Heather Buschman: /* Acknowledgements */

Siglec-8 is a human siglec expressed predominantly on eosinophils and mast cells, and is a paradigm for the rapidly evolving sub-family of CD33-related siglecs that are expressed on various white blood cells<ref>Crocker, P. R., Paulson, J. C. & Varki, A. Siglecs and their roles in the immune system. Nat Rev Immunol 7, 255-266 (2007).</ref><ref>Kikly, K.K., Bochner, B.S., et al. [http://www.ncbi.nlm.nih.gov/pubmed/10856141 Identification of SAF-2, a novel siglec expressed on eosinophils, mast cells, and basophils.] J Allergy Clin Immunol 105, 1093-100 (2000)</ref><ref name="Bochner 2009">Bochner, B.S. [http://www.ncbi.nlm.nih.gov/pubmed/19178537 Siglec-8 on human eosinophils and mast cells, and Siglec-F on murine eosinophils, are functionally related inhibitory receptors.] Clin Exp Allergy 39, 317-324 (2009).</ref><ref>Floyd, H. et al. Siglec-8. A novel eosinophil-specific member of the immunoglobulin superfamily. J Biol Chem 275, 861-866 (2000).</ref>. A characteristic feature of Siglec-8 and most other CD33-related siglecs is a cytoplasmic domain with a single immunoreceptor tyrosine inhibitory motif (ITIM) and a single ITIM-like motif that participate in siglec-mediated regulation of cell signaling and endocytosis. While there is no clear ortholog in mice, Siglec-F has been documented as a functional paralog that has a similar expression pattern on murine leukocytes and similar ligand specificity<ref name="Bochner 2009"/><ref>Tateno, H., Crocker, P. R. & Paulson, J. C. Mouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6'-sulfo-sialyl Lewis X as a preferred
glycan ligand. Glycobiology 15, 1125-1135 (2005).</ref><ref>Zhang, M. et al. Defining the in vivo function of Siglec-F, a CD33-related Siglec expressed on mouse
eosinophils. Blood 109, 4280-4287 (2007).</ref>. Siglec-8 and its paralog Siglec-F recognize a ligand containing both sialic acid and sulfate (NeuAcα2-3[6S]Galβ1-4G[Fucα1-3]GlcNAc-), a specificity that is distinct from all other siglecs. Ligation of Siglec-8 (or Siglec-F) with antibodies or polymeric ligands induces apoptosis of eosinophils, suggesting a therapeutic approach for treating eosinophil (or mast cell) mediated disease by targeting Siglec-8<ref>O'Reilly, M. K. & Paulson, J. C. Siglecs as targets for therapy in immune-cell-mediated disease. Trends Pharmacol Sci 30, 240-248 (2009).</ref><ref>Zimmermann, N. et al. Siglec-F antibody administration to mice selectively reduces blood and tissue
eosinophils. Allergy 63, 1156-1163 (2008).</ref><ref>Bochner, B. S. et al. Glycan array screening reveals a candidate ligand for Siglec-8. J Biol Chem 280, 4307-
4312 (2005).</ref><ref>Nutku, E., Aizawa, H., Hudson, S. A. & Bochner, B. S. Ligation of Siglec-8: a selective mechanism for induction of human eosinophil apoptosis. Blood 101, 5014-5020 (2003).</ref>.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
Participating Investigators (PIs) of the CFG have made major contributions to the understanding of the biology of Siglec-8 and its murine paralog, Siglec-F. These include: Bruce Bochner, Nicolai Bovin, Paul Crocker, James Paulson, Ronald Schnaar, Ajit Varki

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===
NeuAcα2-3(6-SO3)Galβ1-4(Fucα1-3)GlcNAc [6'Su-SLeX]
 

=== Cellular expression ===
Human: Eosinophils, Mast Cells, Basophils
 

=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===
Eosinophil apoptosis
Inhibition of mast cell effector release
 

== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Siglec-8&maxresults=20 CFG database search results for Siglec-8].

=== Glycan profiling ===
Glycan structure analysis has been conducted by the CFG for human and mouse eosinophils.

=== Glycogene microarray ===
Analysis has been conducted on glycosyltransferase expression using the glycogene microarray for murine eosinophils.

=== Knockout mouse lines ===

 
=== Glycan array ===
The discovery of the ligand for siglec-8 and its murine paralog, Siglec-F, was made by investigator-initiated resource requests for glycan array analysis and carbohydrate compounds.

== Related GBPs ==
hSiglec-3 (CD33), Siglec-5, Siglec-6, Siglec, 7, Siglec-9, Siglec-10, Siglec-11, Siglec-F, Siglec-E, Siglec-G

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Paul Crocker, James Paulson, Ron Schnaar

MAG

2010-05-13T17:54:59Z

Heather Buschman: /* Acknowledgements */

Myelin-associated glycoprotein (MAG, Siglec-4) is unique among the siglecs in that it is expressed exclusively on neuronal glial cells<ref>Crocker, P. R., Paulson, J. C. & Varki, A. Siglecs and their roles in the immune system. Nat Rev Immunol 7, 255-266 (2007).</ref><ref name="Schnaar 2009">Schnaar, R. L. Brain gangliosides in axon-myelin stability and axon regeneration. FEBS Lett (2009).</ref>. It is the most highly conserved among the siglecs in mammalian species. This siglec paradigm is unique in its activity for stabilizing axon-myelin interactions. MAG has a cytoplasmic domain that is devoid of ITIMs, but contains a tyrosine-based motif associated with binding the FYN tyrosine kinase, believed to play a role in its activity in myelin-axon interactions. MAG recognizes as ligands sialoside sequences found on gangliosides that are abundant in axonal membranes<ref name="Schnaar 2009"/>. It is one of several proteins in myelin that negatively regulate axon outgrowth following tissue injury, an activity that involves MAG ligand interactions. Evidence suggests that inhibition of MAG ligand interactions may enhance neurite outgrowth and repair of injured neurons<ref>Yang, L. J. et al. Sialidase enhances spinal axon outgrowth in vivo. Proc Natl Acad Sci U S A 103, 11057-11062 (2006).</ref><ref>Vyas, A. A., Blixt, O., Paulson, J. C. & Schnaar, R. L. Potent glycan inhibitors of myelin-associated
glycoprotein enhance axon outgrowth in vitro. J Biol Chem 280, 16305-16310 (2005).</ref>.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
Several CFG Participating Investigators (PIs) have contributed to identification of MAG as a siglec and to understanding the functions of MAG, including: Paul Crocker, Sørge Kelm, James Paulson, Ronald Schnaar

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===
Myelinating cells like oligodendrocytes or Schwann cells

 

=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Siglec-4&maxresults=20 CFG database search results for Siglec-4].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
The CFG has [https://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotyped] the MAG-deficient mouse.

=== Glycan array ===
Investigators have used CFG carbohydrate compounds to study MAG ligand specificity.

== Related GBPs ==
None.

 
This is a test to upload image here [[Image:testImage.jpg]]
 

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Paul Crocker, Sorge Kelm, James Paulson, Ron Schnaar

F17G/GafD

2010-05-13T17:53:54Z

Heather Buschman: /* Acknowledgements */

The F17-G (GafD) adhesin at the tip of flexible F17 fimbriae of enterotoxigenic ''Escherichia coli'' mediates binding to N-acetyl-β-D-glucosamine-presenting receptors on the microvilli of the intestinal epithelium of ruminants, leading to diarrhea or septicaemia. F17-G belong to two-domain adhesins (TDA)s consisting of a pilin domain and a lectin domain, both having an Ig-fold joined via a short interdomain linker<ref>Buts, L., Bouckaert, J., De Gents, E., Loris, R., Oscarson, S., Lahmann, M., Messens, J., Brosens, E., Wyns, L. & De Greve, H. (2003). The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine. Mol. Microb. 49, 705-715.</ref><ref>Merckel, M. C., Tanskanen, J., Edelman, S., Westerlund-Wilkström, B., Korhonen, T. K. & Goldman, A. (2003). The structural basis of receptor-binding by Escherichia coli associaed with diarrhea and septicemia. J. Mol. Biol. 331, 897-905.</ref>. Related adhesins have been characterized in enteropathogenic ''E. coli'' ( FedF on F18 fimbriae<ref>Coddens, A., Diswall, M., Angstrom, J., Breimer, M. E., Goddeeris, B., Cox, E. & Teneberg, S. (2009). Recognition of blood group ABH type 1 determinants by the FedF adhesin of F18-fimbriated Escherichia coli. J Biol Chem 284, 9713-26.</ref> and CfaE on CFA/I pili<ref>Poole, S. T., McVeigh, A. L., Anantha, R. P., Lee, L. H., Akay, Y. M., Pontzer, E. A., Scott, D. A., Bullitt, E. & Savarino, S. J. (2007). Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway. Mol Microbiol 63, 1372-84.</ref>) ) and uropathogenic ones (FimH on type 1 fimbriae<ref>Bouckaert, J., Berglund, J., Schembri, M., De Gents, E., Cools, L., Wuhrer, M., Hung, C.-S., Pinkner, J., Slättegard, R., Savialov, A., Choudhury, D., Langermann, S., Hultgren, S. J., Wyns, L., Klemm, P., Oscarson, S., Knight, S. D. & De Greve, H. (2005). Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin. Mol. Microb. 55, 441-455.</ref> and PapG on P-pili<ref>Dodson, K. W., Pinkner, J. S., Rose, T., Magnusson, G., Hultgren, S. J. & Waksman, G. (2001). Structural basis of the interaction of the pyelonephritic E. coli adhesin to ist human kideny receptor. Cell 105, 733-743.</ref>). Fimbrial adhesins from other organisms, such as CupB6 from ''Pseudomonas aeruginosa'' are also investigated. All share the immunoglobulin-like fold of the two structural components, despite lack of any sequence identity and diversity in carbohydrate specificity and binding site, and the corresponding pili are assembled by the chaperone-usher pathway<ref>De Greve, H., Wyns, L. & Bouckaert, J. (2007). Combining sites of bacterial fimbriae. Curr Opin Struct Biol 17, 506-12.</ref><ref>Sauer, F. G., Barnhart, M., Choudhury, D., Knight, S. D., Waksman, G. & Hultgren, S. J. (2000). Chaperone-assisted pilus assembly and bacterial attachment. Curr Opin Struct Biol 10, 548-56.</ref>. The paradigm is unique among TAD for his specificity toward GlcNAc. The binding site is located laterally and not at the tip of the pili, therefore the long and flexible F17 fimbriae could intrude between the microvilli of the epithelium, with the binding site of the lectin domain interacting laterally with GlcNAc-containing receptors. Five naturally occurring variants, differing in 1-18 amino acids of the adhesion domain have been identified<ref>De Kerpel, M., Van Molle, I., Brys, L., Wyns, L., De Greve, H. & Bouckaert, J. (2006). N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin. Acta Crystallogr Sect F Struct Biol Cryst Commun 62, 1278-82.</ref>.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
This is an emerging field of investigation and contributions arose from a small number of CFG Participating Investigators (PIs). These include: Esther Bullit, Eric Cox, Anne Imberty, Remy Loris, James Nataro

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=fimbriae&maxresults=20 fimbriae] and [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=pili&maxresults=20 pili].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

 
=== Glycan array ===
The specificity of some of the fimbrial tip adhesins was determined by CFG glycan array analysis ([http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_2358 ''P. gingivalis'' fimbriae], [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_PA_v2_178_11182005 ''E. coli'' FedF adhesin], [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_1106 ''E. coli'' CfaE adhesin from CFA/I pili])

== Related GBPs ==
FedF, CfaE, FimH, PapG, CupB6

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Alisdair Boraston, Julie Bouckaert, Anne Imberty

Parainfluenza virus type 3 hemagglutinin-neuraminidase

2010-05-13T17:52:55Z

Heather Buschman: /* Acknowledgements */

Like influenza, the paramyxoviruses show hemagglutinin and neuraminidase (HN) activities, but in this case, the two activities reside on the same glycoprotein. Structures of three paramyxovirus HNs have been determined; they are Newcastle Disease virus, human parainfluenza type 3, and human parainfluenza type 5 (formerly called SV5). The structures show an identical fold to influenza neuraminidase, with an NA active site that is almost identical to that of influenza. Thus HN is a sialidase that also binds sialylated glycans as receptors for cell entry. Whether there is a separate binding site has been a subject of great controversy that is still not solved. NDV shows sialic acid bound at a second site but the second molecule has not been seen in hPIV3 or hPIV5 HN structures. Mutagenesis and antibody studies suggest one site in some strains and two sites in others, while a second site appeared to be created in hPIV3 by mutagenesis. This lack of understanding of how paramyoviruses enter cells and how new viruses are released has severely hampered development to antivirals targeted to these activities. CFG PIs are investigating the binding and cleavage specificities of HNs and mutants.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
CFG Participating Investigators (PIs) contributing to the understanding of parainfluenza virus type 3 HN include: Gillian Air, Theodore Jardetsky, Matteo Porotto, Charles Russell

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=parainfluenza&maxresults=20 CFG database search results for "parainfluenza"].

=== Glycan profiling ===

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===

 
=== Glycan array ===
There have been many resource requests for glycan array screening of paramyxovirus hemagglutinin-neuraminidase.

== Related GBPs ==
* Other paramyxovirus HNs: some appear to have one site that carries out both activities; others appear to have separate sites.
* Human parainfluenza types 1, 2, 4 and 5
* Newcastle Disease virus
* Mumps virus

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Gillian Air, James Paulson, Matteo Porotto

Galectin-3

2010-05-13T17:51:34Z

Heather Buschman: /* Acknowledgements */

Ficolins/Mannose-binding protein

2010-05-13T17:51:08Z

Heather Buschman: /* Acknowledgements */

Mannose receptor

2010-05-13T17:50:20Z

Heather Buschman: /* Acknowledgements */

The mannose receptor represents a paradigm for the involvement of C-type lectins in clearance of circulating glycoproteins. The role of glycan-binding receptors as tags for uptake and turnover was one of the first established functions for endogenous sugar-binding proteins and provides a key model for how glycans can modulate communication between cells in a physiological context. While the asialoglycoprotein receptor would be considered the founder member of this group of receptors, the ''in vivo'' evidence for its function is less compelling than the results for the mannose receptor, which has well defined roles in clearance of sulfated glycoprotein hormones and mannose-bearing glycoproteins released at sites of inflammation.

== CFG Participating Investigators contributing to the understanding of this paradigm ==
As in the case of [[P-Selectin]], much of the evidence for functions of the mannose receptor pre-dates the CFG. However, there have been some further developments for this receptor and other related glycan-binding proteins (GBPs). PIs have generated and characterized knockout mice, defined the sugar-binding specificities, demonstrated clearance ''in vivo'' and endocytosis in tissue culture, and performed structural analyses.

PIs working with the mannose receptor include: Kurt Drickamer, Ten Feizi, Reiko Lee, Yuan Lee, Michel Nussenzweig, Pauline Rudd, Nathalie Scholler, Maureen Taylor, Bill Weis, Chi-Huey Wong

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=%22mannose+receptor%22&maxresults=20 CFG database search results for "mannose receptor"].

=== Glycan profiling ===

 
=== Glycogene microarray ===
The CFG analyzed patterns of mannose receptor expression.

=== Knockout mouse lines ===
Before funding for knockout mice was discontinued, the CFG developed the [https://www.functionalglycomics.org/static/consortium/resources/DataCoreFSR.shtml DNA construct] to create a mouse line lacking the scavenger receptor. The construct can now be obtained from the [http://www.mmrrc.org/catalog/StrainCatalogSearchForm.jsp Mutant Mouse Regional Resource Center (MMRRC)] at the University of California, Davis.

=== Glycan array ===
The CFG analyzed the binding specificities of the mannose receptor.

== Related GBPs ==
Asialoglycoprotein receptor, scavenger receptor C-type lectin, Kupffer cell receptor

== References ==
<references/>
* Coombs PJ, Taylor ME, Drickamer K (2006) Two categories of mammalian galactose-binding receptors distinguished by glycan array profiling. Glycobiology 16, 1C-7C.
* Feinberg H, Taylor ME, Weis WI (2007) Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism. J Biol Chem 282, 17250-17258.
* Coombs PJ, Graham SA, Drickamer K, Taylor ME (2005) Selective binding of the scavenger receptor C-type lectin to Lewisx trisaccharide and related glycan ligands. J Biol Chem 280, 22993-22999.

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Maureen Taylor, Yvette van Kooyk

Galectin-1

2010-05-13T16:58:33Z

Heather Buschman:

Galectin-1

2010-05-13T16:57:45Z

Heather Buschman:

Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of Galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
 
In addition, Galectin-1...
* was the first prototypic galectin for which a function was identified.
* was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte development and increased susceptibility to autoimmune disease.
* is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential.
* has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status<ref>Stowell SR, ''et al''. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. ''J Biol Chem'' 284, 4989-4999 (2009).</ref><ref name="Leppanen 2005">Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. ''J Biol Chem'' 280, 5549-5562 (2005). </ref>.
* binds novel N- and O-glycan determinants that are involved in cell signaling<ref name="Leppanen 2005" /><ref>Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. ''J Biol Chem'' 285, 2232-2244 (2010).</ref><ref>Song X, ''et al''. Novel fluorescent glycan microarray strategy reveals ligands for galectins. ''Chem Biol'' 16, 36-47 (2009).</ref><ref name="Cooper 2008">Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. ''J Leukoc Biol'' 83, 1459-1466 (2008).</ref><ref>Stillman BN, ''et al''. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death.'' J Immunol'' 176, 778-789 (2006).</ref>.
* demonstrates novel distributions in muscle cells versus non-muscle cells<ref>Dias-Baruffi M, ''et al''. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. ''Glycobiology'' '''In Press'''. (2010).</ref>.
* ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes<ref>Cha SK, ''et al''. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. ''Proc Natl Acad Sci U S A'' 105, 9805-9810 (2008).</ref>.
* is involved in lymphocyte trafficking and leukocyte recruitment<ref name="Cooper 2008" /><ref>Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. ''Faseb J'' 22, 682-690 (2008). </ref>.

 
== CFG Participating Investigators contributing to the understanding of this paradigm ==

CFG Participating Investigators (PIs) contributing to the understanding of Galectin-1 include: Linda Baum, C. Fred Brewer, Richard Cummings, Anne Dell, Ten Feizi, M.G. Finn, Thomas Gerken, Benhur Lee, J. Michael Pierce, Mauro Perretti, Gabriel Rabinovich, James Rini, Sachiko Sato, Gerald Schwarting, Pamela Stanley, Victor Thijssen, Gerardo Vasta, John Wang

== Progress toward understanding this GBP paradigm ==

=== Carbohydrate ligands ===

 
=== Cellular expression ===

 
=== Structure ===

 
=== Biological roles of GBP-ligand interaction ===

 
== CFG resources used in investigations ==
The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=galectin-1&maxresults=20 CFG database search results for Galectin-1].

=== Glycan profiling ===

This is a test.

 
=== Glycogene microarray ===

 
=== Knockout mouse lines ===
CFG-generated [http://www.functionalglycomics.org/static/consortium/resources/resourcecoref6.shtml Galectin-1 knockout mice] have been used to study the biological functions of this paradigm GBP. The [http://www.functionalglycomics.org/glycomics/publicdata/phenotyping.jsp phenotype] of Galectin-1 knockout mice was analyzed by the CFG.

=== Glycan array ===
Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of Galectin-1.

== Related GBPs ==
Galectins-2, -5, -7, -10, -11, -13, and -14

== References ==
<references/>

== Acknowledgements ==
The CFG is grateful to the following PIs for their contributions to this wiki page: Linda Baum, Richard Cummings

User:Heather Buschman

2010-05-12T21:17:14Z

Heather Buschman: Blanked the page

User talk:Minoru Fukuda

2010-05-12T21:09:51Z

Heather Buschman: Welcome!

'''Welcome to ''CFGparadigms''!''' We hope you will contribute much and well.
You'll probably want to read the [[Help:Contents|help pages]]. Again, welcome and have fun! [[User:Heather Buschman|Heather Buschman]] 21:09, 12 May 2010 (UTC)

User:Minoru Fukuda

2010-05-12T21:09:51Z

Heather Buschman: Creating user page with biography of new user.

invited author P Selectin: CFG paradigm

User talk:Peter Lipke

2010-05-12T21:09:39Z

Heather Buschman: Welcome!

User:Peter Lipke

2010-05-12T21:09:39Z

Heather Buschman: Creating user page with biography of new user.

Professor and Chairperson of Biology at Brooklyn College, CUNY. I have a B.S. in Chemistry from U. Chicago in 1971, a PhD in Biochemistry from U. California Berkeley with C.E. Ballou, I was a post-doc in zoology at U. Wisconsin with Jack Lilien. I was Asst. Prof. through Prof. of Biology at Hunter College CUNY before moving to Brooklyn College in 2006.

My lab works on structure-function of fungal cell adhesion proteins, including recent work on role of amyloid sequences in cell-cell adhesion and host-pathogen interactions. Most of this work has been with Ig-superfamily adhesins, but recently we have started work on the Flo families of lectins as well. We also work and publish on fungal cell wall biogenesis and evolution, using genomic and bioinformatic approaches.

User talk:Ron Schnaar

2010-05-12T17:50:20Z

Heather Buschman: Welcome!

User:Ron Schnaar

2010-05-12T17:50:20Z

Heather Buschman: Creating user page with biography of new user.

Invited author

User talk:Tamara Doering

2010-05-12T16:51:13Z

Heather Buschman: Welcome!

User:Tamara Doering

2010-05-12T16:51:13Z

Heather Buschman: Creating user page with biography of new user.

Tamara Doering was an undergraduate at Johns Hopkins University, where she worked in the labs of Michael Edidin and Saul Roseman. She went on to the MSTP program at Johns Hopkins Medical School, where she worked with Paul Englund and Gerald Hart in the Department of Biological Chemistry. Her thesis work was on GPI anchor biosynthesis in African trypanosomes, and she received her degrees in 1991. Her postdoctoral fellowship (1993-6), during which she studied ER to Golgi transport of GPI-anchored proteins in Saccharomyces cerevisiae, was with Randy Schekman at the University of California at Berkeley. She visited Arturo Casadevall's lab at the Albert Einstein College of Medicine for part of the 1996-1997 academic year to get acquainted with her new microbe of choice, Cryptococcus neoformans, before joining the faculty in Pharmacology at Cornell Medical College in the fall of 1997. In the fall of 1999 she moved her lab to the faculty of Molecular Microbiology at Washington University medical school, where she was promoted to Associate Professor in 2004 and became director of the Graduate Program in Molecular Microbiology and Microbial Pathogenesis in 2007. Her work covers aspects of the biochemistry, cell and molecular biology of C. neoformans, in particular related to its polysaccharide capsule, as well as issues of capsule regulation and host cell interactions.

Quick guide to editing

2010-05-11T21:26:48Z

Heather Buschman: Created page with 'To format a wiki page, use common html tags for bold, italics, lists, symbols, hyperlinks, etc, or use the buttons above the editing box for shortcuts. For quick reference, …'

To format a wiki page, use common html tags for bold, italics, lists, symbols, hyperlinks, etc, or use the buttons above the editing box for shortcuts.
 
For quick reference, see this [http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf guide to wiki formatting].

MediaWiki:Sidebar

2010-05-11T21:21:47Z

Heather Buschman:

* SEARCH

* Navigation
** mainpage|mainpage
** quick guide to editing|Quick guide to editing
** recentchanges-url|recentchanges
** more help|More help

MediaWiki:Sidebar

2010-05-11T21:20:54Z

Heather Buschman:

* SEARCH

* Navigation
** mainpage|mainpage
** wiki editing cheat sheet|Wiki editing cheat sheet
** recentchanges-url|recentchanges
** more help|More help

MediaWiki:Sidebar

2010-05-11T21:19:17Z

Heather Buschman:

MediaWiki:Sidebar

2010-05-11T21:16:45Z

Heather Buschman:

CFGparadigms:About

2010-05-11T21:16:04Z

Heather Buschman:

The purpose of the CFG Paradigm Pages is to demonstrate the involvement and impact the CFG Participating Investigators (PIs) and the scientific cores have made towards the CFG's overall goal to 'define paradigms by which protein-carbohydrate interactions mediate cell communication.'

 
Instructions can be found [http://www.functionalglycomics.org/static/consortium/CFGParadigm.shtml here].

MediaWiki:Sidebar

2010-05-11T21:13:48Z

Heather Buschman:

More help

2010-05-11T21:12:25Z

Heather Buschman: Created page with ''''How to edit the CFG Paradigm Pages:''' * Visit the [http://glycobank.mit.edu/glycoWiki/Main_PageCFG Main Page] and click the 'Log in' link in the top right-hand corner, or vis…'

'''How to edit the CFG Paradigm Pages:'''
* Visit the [http://glycobank.mit.edu/glycoWiki/Main_PageCFG Main Page] and click the 'Log in' link in the top right-hand corner, or visit the [http://glycobank.mit.edu/wiki/mediawiki-1.15.1/index.php?title=Special:UserLogin&returnto=Main_Page Log in] page directly.
* Create a login and password (enter any text in the 'biography' box) and wait for administrative approval.
* From the [http://glycobank.mit.edu/glycoWiki/Main_Page CFG Wiki Main Page], find the paradigm GBP you are interested in. Follow the link to that page.
* Click the 'edit' tab at the top of the page.
* You will see a text box containing all of the text and html tags that make up that paradigm page.
* Contribute 2-3 sentences for each of the blank fields (e.g. 'Progress toward understanding this GBP paradigm').
* If you can, contribute to the 'CFG resources used in investigations' section, including links to specific datasets in the [http://www.functionalglycomics.org CFG database].
* For formatting, use common html tags ([http://www.functionalglycomics.org/static/consortium/Paradigms/WikiCodes.pdf see table]). ''Tip: Copy and paste text from the edit box of another Wiki page that contains the formatting style you would like to emulate.''
* Click 'Show preview' below the editing box.
* When finished, click 'Save page'.
* For more help editing Wiki pages, visit the [http://en.wikipedia.org/wiki/Help:Wiki_markup Wikipedia markup help page].

Help:Contents

2010-05-11T21:10:39Z

Heather Buschman: