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4yg3

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Revision as of 06:14, 6 October 2017

Structural basis of glycan recognition in neonate-specific rotaviruses

Structural highlights

4yg3 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4yfw, 4ye2, 4yez, 4yg0, 4yg6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VP4_ROTBB] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity). VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact (By similarity).

Publication Abstract from PubMed

Strain-dependent variation of glycan recognition during initial cell attachment of viruses is a critical determinant of host specificity, tissue-tropism and zoonosis. Rotaviruses (RVs), which cause life-threatening gastroenteritis in infants and children, display significant genotype-dependent variations in glycan recognition resulting from sequence alterations in the VP8* domain of the spike protein VP4. The structural basis of this genotype-dependent glycan specificity, particularly in human RVs, remains poorly understood. Here, from crystallographic studies, we show how genotypic variations configure a novel binding site in the VP8* of a neonate-specific bovine-human reassortant to uniquely recognize either type I or type II precursor glycans, and to restrict type II glycan binding in the bovine counterpart. Such a distinct glycan-binding site that allows differential recognition of the precursor glycans, which are developmentally regulated in the neonate gut and abundant in bovine and human milk provides a basis for age-restricted tropism and zoonotic transmission of G10P[11] rotaviruses.

Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus.,Hu L, Ramani S, Czako R, Sankaran B, Yu Y, Smith DF, Cummings RD, Estes MK, Venkataram Prasad BV Nat Commun. 2015 Sep 30;6:8346. doi: 10.1038/ncomms9346. PMID:26420502^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hu L, Ramani S, Czako R, Sankaran B, Yu Y, Smith DF, Cummings RD, Estes MK, Venkataram Prasad BV. Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus. Nat Commun. 2015 Sep 30;6:8346. doi: 10.1038/ncomms9346. PMID:26420502 doi:http://dx.doi.org/10.1038/ncomms9346

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4yg3"

@@ Line 1: / Line 1: @@
 ==Structural basis of glycan recognition in neonate-specific rotaviruses==
 <StructureSection load='4yg3' size='340' side='right' caption='[[4yg3]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yfw|4yfw]], [[4ye2|4ye2]], [[4yez|4yez]], [[4yg0|4yg0]], [[4yg6|4yg6]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg3 OCA], [http://pdbe.org/4yg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4yg3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg3 OCA], [http://pdbe.org/4yg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4yg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yg3 ProSAT]</span></td></tr>
 </table>
 == Function ==

4yg3

From Proteopedia

Revision as of 06:14, 6 October 2017

Structural basis of glycan recognition in neonate-specific rotaviruses

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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