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==Functional and structural characterization of P[19] rotavirus VP8* interaction with histo-blood group antigens== | |||
<StructureSection load='5ymt' size='340' side='right'caption='[[5ymt]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ymt]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_rotavirus_A Human rotavirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YMT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.199Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5ymt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ymt OCA], [https://pdbe.org/5ymt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ymt RCSB], [https://www.ebi.ac.uk/pdbsum/5ymt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ymt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9Q2P6_9VIRU Q9Q2P6_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rotaviruses (RVs), which cause severe gastroenteritis in infants and children, recognize glycan ligands in a genotype-dependent manner via the distal VP8* head of the spike protein VP4. However, the glycan binding mechanisms remain elusive for the P[II] genogroup RVs, including the widely prevalent human RVs (P[8], P[4], and P[6]) and a rare P[19] RV. In this study, we characterized the glycan binding specificity of human and porcine P[6]/P[19] RV VP8* and found that the P[II] genogroup RV VP8*s could commonly interact with mucin core 2 which may play an important role in the RV evolution and cross-species transmission. We determined the first P[6] VP8* structure, as well as the complex structures of human P[19] VP8* with core 2 and lacto-N-tetraose (LNT). A glycan binding site was identified in human P[19] VP8*. Structural superimposition and sequence alignment revealed the conservation of the glycan binding site in the P[II] genogroup RV VP8*s. Our data provide significant insight into the glycan binding specificity and glycan binding mechanism of the P[II] genogroup RV VP8*s, which would help understanding of RV evolution, transmission, epidemiology, and vaccine approach.IMPORTANCERotaviruses (RVs), belonging to the family Reoviridae, are double-stranded RNA viruses causing acute gastroenteritis in children and animals worldwide. Depending on phylogeny of the VP8* sequences, P[6] and P[19] RVs are grouped into the genogroup II together with P[4] and P[8] that are widely prevalent in humans. In this study, we characterized the glycan binding specificity of human and porcine P[6]/P[19] RV VP8*s, determined the crystal structure of P[6] VP8*, and uncovered the glycan binding pattern in P[19] VP8*, revealing a conserved glycan binding site in the VP8*s of P[II] genogroup RVs by structural superimposition and sequence alignment. Our data suggested that mucin core 2 may play an important role in the P[II] RV evolution and cross-species transmission. These data provide insight into cell attachment, infection, epidemiology, and evolution of P[II] genogroup RVs, which would help to develop control and prevention strategies against RVs. | |||
Glycan Binding Specificity and Mechanism of Human and Porcine P[6]/P[19] Rotavirus VP8*s.,Sun X, Li D, Qi J, Chai W, Wang L, Wang L, Peng R, Wang H, Zhang Q, Pang L, Kong X, Wang H, Jin M, Gao GF, Duan Z J Virol. 2018 May 2. pii: JVI.00538-18. doi: 10.1128/JVI.00538-18. PMID:29720519<ref>PMID:29720519</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Duan | <div class="pdbe-citations 5ymt" style="background-color:#fffaf0;"></div> | ||
[[Category: Sun | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human rotavirus A]] | |||
[[Category: Large Structures]] | |||
[[Category: Duan Z]] | |||
[[Category: Sun X]] | |||
Latest revision as of 11:33, 22 November 2023
Functional and structural characterization of P[19] rotavirus VP8* interaction with histo-blood group antigensFunctional and structural characterization of P[19] rotavirus VP8* interaction with histo-blood group antigens
Structural highlights
FunctionPublication Abstract from PubMedRotaviruses (RVs), which cause severe gastroenteritis in infants and children, recognize glycan ligands in a genotype-dependent manner via the distal VP8* head of the spike protein VP4. However, the glycan binding mechanisms remain elusive for the P[II] genogroup RVs, including the widely prevalent human RVs (P[8], P[4], and P[6]) and a rare P[19] RV. In this study, we characterized the glycan binding specificity of human and porcine P[6]/P[19] RV VP8* and found that the P[II] genogroup RV VP8*s could commonly interact with mucin core 2 which may play an important role in the RV evolution and cross-species transmission. We determined the first P[6] VP8* structure, as well as the complex structures of human P[19] VP8* with core 2 and lacto-N-tetraose (LNT). A glycan binding site was identified in human P[19] VP8*. Structural superimposition and sequence alignment revealed the conservation of the glycan binding site in the P[II] genogroup RV VP8*s. Our data provide significant insight into the glycan binding specificity and glycan binding mechanism of the P[II] genogroup RV VP8*s, which would help understanding of RV evolution, transmission, epidemiology, and vaccine approach.IMPORTANCERotaviruses (RVs), belonging to the family Reoviridae, are double-stranded RNA viruses causing acute gastroenteritis in children and animals worldwide. Depending on phylogeny of the VP8* sequences, P[6] and P[19] RVs are grouped into the genogroup II together with P[4] and P[8] that are widely prevalent in humans. In this study, we characterized the glycan binding specificity of human and porcine P[6]/P[19] RV VP8*s, determined the crystal structure of P[6] VP8*, and uncovered the glycan binding pattern in P[19] VP8*, revealing a conserved glycan binding site in the VP8*s of P[II] genogroup RVs by structural superimposition and sequence alignment. Our data suggested that mucin core 2 may play an important role in the P[II] RV evolution and cross-species transmission. These data provide insight into cell attachment, infection, epidemiology, and evolution of P[II] genogroup RVs, which would help to develop control and prevention strategies against RVs. Glycan Binding Specificity and Mechanism of Human and Porcine P[6]/P[19] Rotavirus VP8*s.,Sun X, Li D, Qi J, Chai W, Wang L, Wang L, Peng R, Wang H, Zhang Q, Pang L, Kong X, Wang H, Jin M, Gao GF, Duan Z J Virol. 2018 May 2. pii: JVI.00538-18. doi: 10.1128/JVI.00538-18. PMID:29720519[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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