Mannose receptor - Revision history

Kurt Drickamer: /* Related GBPs */

2011-04-16T09:12:54Z

Related GBPs

Kurt Drickamer: /* Knockout mouse lines */

2011-04-16T09:12:25Z

Knockout mouse lines

Carole Weaver: /* Related GBPs */

2011-03-18T21:58:46Z

Related GBPs

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:56:42Z

Biosynthesis of ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:56:09Z

Biosynthesis of ligands

Kurt Drickamer: /* Carbohydrate ligands */

2011-03-17T18:55:13Z

Carbohydrate ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:49:32Z

Biosynthesis of ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:46:02Z

Biosynthesis of ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:45:33Z

Biosynthesis of ligands

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-17T18:30:38Z

Biosynthesis of ligands

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 == Related GBPs ==
-Asialoglycoprotein receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=asialoglycoprotein+AND+receptor&maxresults=20 (CFG data)], scavenger receptor C-type lectin [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=scavenger+AND+receptor+AND+C-type+AND+lectin&maxresults=20 (CFG data)], Kupffer cell receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Kupffer+AND+cell+AND+receptor&maxresults=20 (CFG data)], Endo-180
+Asialoglycoprotein receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=asialoglycoprotein+AND+receptor&maxresults=20 (CFG data)], scavenger receptor C-type lectin [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=scavenger+AND+receptor+AND+C-type+AND+lectin&maxresults=20 (CFG data)], Kupffer cell receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Kupffer+AND+cell+AND+receptor&maxresults=20 (CFG data)], Endo-180.
 == References ==

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 === 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 C-type lectin. 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.
+Mice lacking the mannose receptor have been described.<ref name="Swain2003">Swain, SD, Lee, SJ, Nussenzweig, MC, and Harmsen, AG (2003) Absence of the macrophage mannose receptor in mice does not increase susceptibility to <i>Pneumocystis carinii</i> infection in vivo. Infect. Immun. 71, 6213-6221</ref> 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 C-type lectin. 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 ===

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 == Related GBPs ==
-Asialoglycoprotein receptor, scavenger receptor C-type lectin, Kupffer cell receptor, Endo-180
+Asialoglycoprotein receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=asialoglycoprotein+AND+receptor&maxresults=20 (CFG data)], scavenger receptor C-type lectin [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=scavenger+AND+receptor+AND+C-type+AND+lectin&maxresults=20 (CFG data)], Kupffer cell receptor [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=Kupffer+AND+cell+AND+receptor&maxresults=20 (CFG data)], Endo-180
 == References ==

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 High mannose oligosaccharides on released lysosomal enzymes are generated from mannose 6-phosphate-containing oligosaccharides ([http://www.functionalglycomics.org/CFGparadigms/index.php/Cation-dependent_Mannose-6-phosphate_receptor M6PR]) by phosphatase activity.
 <br><br>
-<b>Glycans on pathogens</b><br>
+<b>Glycans on micro-organisms</b><br>
 Biosynthesis mannans on fungi has been well studied in a number of species. For example, in the yeast <i>S. cerevisiae</i>, the KRE2/MNT1 genes encode mannosyltransferases that synthesize both N- and O-linked mannans.<ref name”Lussier1999”>Lussier, M, Sdicu, A-M and Bussey, H (1999) The KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1426, 323-334</ref>
 <br><br>

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 <br><br>
 <b>Glycans on pathogens</b><br>
-The biosynthesis pathways for the bacterial lipopolysaccharides have been extensively studied and the gene families responsible for the expression of different glycan sequences have been characterized.<ref name”Raetz2002”>Raetz CR and Whitfield C (2002) Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71, 635-700</ref>
+Biosynthesis mannans on fungi has been well studied in a number of species. For example, in the yeast <i>S. cerevisiae</i>, the KRE2/MNT1 genes encode mannosyltransferases that synthesize both N- and O-linked mannans.<ref name”Lussier1999”>Lussier, M, Sdicu, A-M and Bussey, H (1999) The KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1426, 323-334</ref>
 <br><br>
 The mycobacterial transferases for synthesis of the lipo-arabinomannan (LAM) core and the extended ManLAM structures have been characterized.<ref name”Tam2009”>Tam, P-H and Lowary, TL (2009) Recent advances in mycobacterial cell wall glycan biosynthesis. Cur. Opin Struct. Biol. 13, 618-625</ref>
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 === Carbohydrate ligands ===
-The multiple domains in the extracellular region of the mannose receptor allow recognition of a diverse range of glycoconjugate ligands<ref name="Taylor 1990">Taylor, ME, Conary, JT, Lennartz, MR, Stahl, PD, Drickamer, K (1990) Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains.<i>J Biol Chem</i> <b> 265</b>,12156-12162</ref>. Several of the eight C-type carbohydrate-recognition domains are involved in Ca2+-dependent recognition of terminal mannose, GlcNAc or fucose residues on the oligosaccharides of endogenous glycoproteins or the surfaces of microorganisms<ref name="Taylor 1992">Taylor, ME., Bezouska, K, Drickamer, K (1992) Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. <i>J Biol Chem</i> <b>267</b>, 1710-1726</ref><ref name="Mullin 1997">Mullin, NP, Hitchen, PG, Taylor, ME (1997) Mechanism of Ca2+- and monosaccharide-binding to a C-type carbohydrate-recognition domain of the macrophage mannose receptor. <i>J Biol Chem</i> <b>272</b>, 5668-5681</ref>, while the R-type carbohydrate-recognition domain binds sulfated GalNAc and sulfated galactose residues<ref name="Fiete 1998">Fiete DJ, Beranek MC, Baenziger JU (1998) A cysteine-rich domain of the "mannose" receptor mediates GalNAc-4-SO4 binding. <i>Proc Natl Acad Sci USA</i> <b>95</b>, 2089-2093</ref>. Biological ligands for the mannose receptor include lysosomal hydrolases, the pro-collagen peptides of type I and type III collagens and tissue plasminogen activator – proteins that bear high mannose oligosaccharides and are released from cells at sites of inflammation<ref name="Lee 2002">Lee SJ, Evers S, Roeder D, Parlow AF, Risteli J, Risteli L, Lee YC, Feizi T, Langen H, Nussenzweig MC (2002) Mannose receptor-mediated regulation of serum glycoprotein homeostasis. <i>Science</i> <b>295</b>, 1898-1901</ref>. The main biological ligands recognized by the R-type carbohydrate-recognition domain are the pituitary hormones lutropin and thyrotropin which bear oligosaccharides terminating in GalNAc-4-SO4<ref name="Fiete 1998"/><ref name="Liu 2000">Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ. (2000) Crystal structure of the cysteine-rich domain of the mannose receptor complexed with a sulfated carbohydrate ligand. <i>J Exp Med</i> <b>191</b>, 1105-1116</ref>.The CFG contributed to defining specificity for oligosaccharides through screening of glycan arrays<ref name="Hsu 2009">Hsu TL, Cheng SC, Yang WB, Chin SW, Chen BH, Huang MT, Hsieh SL, Wong CH (2009) Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins. <i>J Biol Chem</i> <b>284</b>, 34479-34489</ref>.
+The multiple domains in the extracellular region of the mannose receptor allow recognition of a diverse range of glycoconjugate ligands<ref name="Taylor 1990">Taylor, ME, Conary, JT, Lennartz, MR, Stahl, PD, Drickamer, K (1990) Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains.<i>J Biol Chem</i> <b> 265</b>,12156-12162</ref>. Several of the eight C-type carbohydrate-recognition domains are involved in Ca<sup>2+</sup>-dependent recognition of terminal mannose, GlcNAc or fucose residues on the oligosaccharides of endogenous glycoproteins or the surfaces of microorganisms<ref name="Taylor 1992">Taylor, ME., Bezouska, K, Drickamer, K (1992) Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. <i>J Biol Chem</i> <b>267</b>, 1710-1726</ref><ref name="Mullin 1997">Mullin, NP, Hitchen, PG, Taylor, ME (1997) Mechanism of <sup>2+</sup>- and monosaccharide-binding to a C-type carbohydrate-recognition domain of the macrophage mannose receptor. <i>J Biol Chem</i> <b>272</b>, 5668-5681</ref>, while the R-type carbohydrate-recognition domain binds sulfated GalNAc and sulfated galactose residues<ref name="Fiete 1998">Fiete DJ, Beranek MC, Baenziger JU (1998) A cysteine-rich domain of the "mannose" receptor mediates GalNAc-4-SO4 binding. <i>Proc Natl Acad Sci USA</i> <b>95</b>, 2089-2093</ref>. Biological ligands for the mannose receptor include lysosomal hydrolases, the pro-collagen peptides of type I and type III collagens and tissue plasminogen activator – proteins that bear high mannose oligosaccharides and are released from cells at sites of inflammation<ref name="Lee 2002">Lee SJ, Evers S, Roeder D, Parlow AF, Risteli J, Risteli L, Lee YC, Feizi T, Langen H, Nussenzweig MC (2002) Mannose receptor-mediated regulation of serum glycoprotein homeostasis. <i>Science</i> <b>295</b>, 1898-1901</ref>. The main biological ligands recognized by the R-type carbohydrate-recognition domain are the pituitary hormones lutropin and thyrotropin which bear oligosaccharides terminating in GalNAc-4-SO4<ref name="Fiete 1998"/><ref name="Liu 2000">Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ. (2000) Crystal structure of the cysteine-rich domain of the mannose receptor complexed with a sulfated carbohydrate ligand. <i>J Exp Med</i> <b>191</b>, 1105-1116</ref>.The CFG contributed to defining specificity for oligosaccharides through screening of glycan arrays<ref name="Hsu 2009">Hsu TL, Cheng SC, Yang WB, Chin SW, Chen BH, Huang MT, Hsieh SL, Wong CH (2009) Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins. <i>J Biol Chem</i> <b>284</b>, 34479-34489</ref>.
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 === Biosynthesis of ligands ===
 <br>
 === Structure ===