Cyanovirin-N (CVN) - Revision history

Kurt Drickamer: /* Biosynthesis of ligands */

2011-04-08T09:16:24Z

Biosynthesis of ligands

Angela Gronenborn: /* Biosynthesis of ligands */

2011-04-04T16:48:20Z

Biosynthesis of ligands

Angela Gronenborn: /* Biosynthesis of ligands */

2011-04-04T15:38:23Z

Biosynthesis of ligands

Carole Weaver: /* Glycogene microarray */

2011-03-30T23:26:12Z

Glycogene microarray

Carole Weaver: /* Related GBPs */

2011-03-22T17:54:43Z

Related GBPs

Carole Weaver at 22:05, 21 September 2010

2010-09-21T22:05:12Z

Carole Weaver at 18:17, 2 July 2010

2010-07-02T18:17:22Z

Carole Weaver at 23:54, 21 June 2010

2010-06-21T23:54:12Z

Jim Paulson at 21:22, 19 June 2010

2010-06-19T21:22:51Z

Angela Gronenborn: /* Related GBPs */

2010-06-12T22:29:37Z

Related GBPs

@@ Line 22: / Line 22: @@
 === Biosynthesis of ligands ===
 <br>
 === Structure ===

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 === Biosynthesis of ligands ===
 <br>
-The envelope glycans of immunodeficiency virions, that are ligands for CV-N and the CVNH family members, are almost entirely oligomannose antigens. There are radical differences between recombinant and viral gp120 envelope glycosylation. The glycosylation of recombinant gp120 reveals an unprocessed intrinsic patch of Man5–9GlcNAc2 glycans, which appears to have resisted α-mannosidase activity. The remaining glycans in the recombinant gp120 are a cell-speciﬁc mixture of complex type glycans. The trimeric viral gp120 contains the original mannose patch. The array of complex glycans is absent in the native viral trimeric gp120, however, and appears to be replaced by a further range of Man5–9GlcNAc2 glycans. See details in Doores et al., PNAS, 2011.
+The envelope glycans of immunodeficiency virions, that are ligands for CV-N and the CVNH family members, are almost entirely oligomannose glycans. There are radical differences between recombinant and viral gp120 envelope glycosylation. The glycosylation of recombinant gp120 reveals an unprocessed intrinsic patch of Man5–9GlcNAc2 glycans, which appears to have resisted α-mannosidase activity. The remaining glycans in the recombinant gp120 are a cell-speciﬁc mixture of complex type glycans. The trimeric viral gp120 contains the original mannose patch. The array of complex glycans is absent in the native viral trimeric gp120 that contains mostly high mannose (Man5–9GlcNAc2) glycans. See details in Doores et al., PNAS, 2011.
 === Structure ===

@@ Line 23: / Line 23: @@
 === Biosynthesis of ligands ===
 <br>
 === Structure ===
 The structures of Cyanovirin-N can be found at http://www.pdb.org/ [http://www.pdb.org/pdb/results/results.do?outformat=&qrid=620C4AC9&tabtoshow=Current].

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 === Glycogene microarray ===
-Analysis has not been conducted.
+Analysis has not been conducted. CVN is not represented on the CFG microarrays, which only contain probes for mouse and human glycogenes.
 === Knockout mouse lines ===

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 == Related GBPs ==
-A large family of CVNHs has been found in both eukaryotic fungi and cyanobacteria (see refs 3, 4 and 5 below).
+A large family of CVNHs has been found in both eukaryotic fungi and cyanobacteria (see refs 3, 4 and 5 below). Click here for [http://www.functionalglycomics.org/glycomics/search/jsp/result.jsp?query=CVNH&cat=coreh CFG data] on CVNHs.
 == References ==

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 === Cellular expression of GBP and ligands ===
-The Cyanovirin-N protein is expressed by Cyanobacterium (blue-green alga) Nostoc ellipsosporum. It binds ligands on glycoproteins of enveloped viruses.
+The Cyanovirin-N protein is expressed by Cyanobacterium (blue-green alga) Nostoc ellipsosporum. It binds ligands on glycoproteins of enveloped viruses including HIV, SIV, Ebola, influenza and hepatitis C.
 === Biosynthesis of ligands ===

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 The physiological ligand for Cyanovirin-N is not precisely known. However, based on extensive data on carbohydrate binding studies on this protein by NMR, X-ray, and glycan microarray screening on the CFG microarray, it is expected that CV-N would recognize any glycans that contain highly enriched alpha (1->2) linkage - mannoses.
-<br>
+=== Cellular expression of GBP and ligands ===
-=== Cellular expression ===
+=== Biosynthesis of ligands ===
 <br>
 === Structure ===
 The structures of Cyanovirin-N can be found at http://www.pdb.org/ [http://www.pdb.org/pdb/results/results.do?outformat=&qrid=620C4AC9&tabtoshow=Current].
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 === Biological roles of GBP-ligand interaction ===
 In vitro, low nanomolar concentrations of either natural or recombinant CV-N irreversibly inactivate diverse laboratory strains and primary isolates of human immunodeficiency virus (HIV) type 1 as well as strains of HIV type 2 and simian immunodeficiency virus<ref name = "Boyd1997"/>.
 == CFG resources used in investigations ==
@@ Line 61: / Line 58: @@
 === Glycogene microarray ===
 Analysis has not been conducted.
 === Knockout mouse lines ===
 Not applicable.
 === Glycan array ===
 The CFG has contributed glycans for various glycan specificity studies.
-Glycan specificity analysis has been conducted for [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_3001 Cyanovirin-N] using the CFG glycan microarray as shown below.
+Glycan specificity analysis has been conducted for [http://www.functionalglycomics.org/glycomics/HServlet?operation=view&sideMenu=no&psId=primscreen_3001 Cyanovirin-N] using the CFG glycan microarray as shown below. To see all glycan array results for Cyanovirin-N, click [http://www.functionalglycomics.org/glycomics/search/jsp/result.jsp?query=cyanovirin-N&cat=coreh here].
 [[File:CVNglycan.png]]