3tb0

From Proteopedia

(Difference between revisions)

Revision as of 07:18, 4 August 2016

Crystal structure of Rhesus Rotavirus VP8* in complex with N-Glycolylneuraminic acid

Structural highlights

3tb0 is a 1 chain structure with sequence from Rotrh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	3tay
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VP4_ROTRH] 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. It is subsequently lost, together with VP7, following virus entry into the host cell. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In sialic acid-dependent and/or integrin-dependent strains, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1.^[1] 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.^[2] 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.^[3]

Publication Abstract from PubMed

The rotavirus spike protein domain VP8* is essential for recognition of cell-surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-acetylneuraminic acids occur naturally in both animals and humans whereas N-glycolylneuraminic acids are present only through dietary uptake in normal human tissues. The preference of animal rotaviruses towards these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* towards N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from porcine rotavirus CRW-8 and bovine rotavirus NCDV showed preference for N-glycolyl- over N-acetylneuraminic acids, contrasting with monkey rotavirus RRV. Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl- or N-glycolyl-moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157 to Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid.

Structural basis of rotavirus strain preference towards N-acetyl- or N-glycolylneuraminic acid-containing receptors.,Yu X, Dang VT, Fleming FE, von Itzstein M, Coulson BS, Blanchard H J Virol. 2012 Oct 3. PMID:23035213^[4]

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

References

↑ Kim IS, Trask SD, Babyonyshev M, Dormitzer PR, Harrison SC. Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry. J Virol. 2010 Jun;84(12):6200-7. doi: 10.1128/JVI.02461-09. Epub 2010 Apr 7. PMID:20375171 doi:http://dx.doi.org/10.1128/JVI.02461-09
↑ Kim IS, Trask SD, Babyonyshev M, Dormitzer PR, Harrison SC. Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry. J Virol. 2010 Jun;84(12):6200-7. doi: 10.1128/JVI.02461-09. Epub 2010 Apr 7. PMID:20375171 doi:http://dx.doi.org/10.1128/JVI.02461-09
↑ Kim IS, Trask SD, Babyonyshev M, Dormitzer PR, Harrison SC. Effect of mutations in VP5 hydrophobic loops on rotavirus cell entry. J Virol. 2010 Jun;84(12):6200-7. doi: 10.1128/JVI.02461-09. Epub 2010 Apr 7. PMID:20375171 doi:http://dx.doi.org/10.1128/JVI.02461-09
↑ Yu X, Dang VT, Fleming FE, von Itzstein M, Coulson BS, Blanchard H. Structural basis of rotavirus strain preference towards N-acetyl- or N-glycolylneuraminic acid-containing receptors. J Virol. 2012 Oct 3. PMID:23035213 doi:http://dx.doi.org/10.1128/JVI.06975-11

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tb0"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Rhesus Rotavirus VP8* in complex with N-Glycolylneuraminic acid==
 <StructureSection load='3tb0' size='340' side='right' caption='[[3tb0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tb0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TB0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tb0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rotrh Rotrh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TB0 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN0:METHYL+3,5-DIDEOXY-5-[(HYDROXYACETYL)AMINO]-D-GLYCERO-ALPHA-D-GALACTO-NON-2-ULOPYRANOSIDONIC+ACID'>MN0</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tay|3tay]]</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=3tb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tb0 RCSB], [http://www.ebi.ac.uk/pdbsum/3tb0 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=3tb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb0 OCA], [http://pdbe.org/3tb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tb0 RCSB], [http://www.ebi.ac.uk/pdbsum/3tb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tb0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3tb0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[VP4|VP4]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhesus rotavirus]]
+[[Category: Rotrh]]
 [[Category: Blanchard, H]]
 [[Category: Yu, X]]

3tb0

From Proteopedia

Revision as of 07:18, 4 August 2016

Crystal structure of Rhesus Rotavirus VP8* in complex with N-Glycolylneuraminic acid

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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