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4yg6

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Structural basis of glycan recognition in neonate-specific rotaviruses

Structural highlights

4yg6 is a 4 chain structure with sequence from Rotavirus A RVA/Cow-tc/USA/B223/1983/G10P11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.46Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VP4_ROTSH 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 (PubMed:1649333). 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 (PubMed:9144247, PubMed:15165605). It is subsequently lost, together with VP7, following virus entry into the host cell (PubMed:15165605). Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts (By similarity).[HAMAP-Rule:MF_04132]^[1] ^[2] ^[3] Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[HAMAP-Rule:MF_04132] Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. 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. In some other strains, VP8* mediates the attachment to histo-blood group antigens (HBGAs) for viral entry.[HAMAP-Rule:MF_04132]

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^[4]

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

References

↑ Anthony ID, Bullivant S, Dayal S, Bellamy AR, Berriman JA. Rotavirus spike structure and polypeptide composition. J Virol. 1991 Aug;65(8):4334-40. PMID:1649333 doi:10.1128/JVI.65.8.4334-4340.1991
↑ Coulson BS, Londrigan SL, Lee DJ. Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells. Proc Natl Acad Sci U S A. 1997 May 13;94(10):5389-94. PMID:9144247 doi:10.1073/pnas.94.10.5389
↑ López S, Arias CF. Multistep entry of rotavirus into cells: a Versaillesque dance. Trends Microbiol. 2004 Jun;12(6):271-8. PMID:15165605 doi:10.1016/j.tim.2004.04.003
↑ 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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4yg6"

Categories: Large Structures | Hu L | Prasad BVV

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4yg6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_A_RVA/Cow-tc/USA/B223/1983/G10P11 Rotavirus A RVA/Cow-tc/USA/B223/1983/G10P11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YG6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.46&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg6 OCA], [https://pdbe.org/4yg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yg6 RCSB], [https://www.ebi.ac.uk/pdbsum/4yg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yg6 ProSAT]</span></td></tr>
 </table>

4yg6

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Current revision

Structural basis of glycan recognition in neonate-specific rotaviruses

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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