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6h9w
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6h9w is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens== | |
| + | <StructureSection load='6h9w' size='340' side='right'caption='[[6h9w]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6h9w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Group_a_rotaviruses Group a rotaviruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28875 Group A rotaviruses])</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=6h9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9w OCA], [http://pdbe.org/6h9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9w RCSB], [http://www.ebi.ac.uk/pdbsum/6h9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rotavirus is the leading agent causing acute gastroenteritis in young children, with the P[8] genotype accounting for more than 80% of infections in humans. The molecular bases for binding of the VP8* domain from P[8] VP4 spike protein to its cellular receptor, the secretory H type-1 antigen (Fuc-alpha1,2-Gal-beta1,3-GlcNAc; H1), and to its precursor lacto-N-biose (Gal-beta1,3-GlcNAc; LNB) have been determined. The resolution of P[8] VP8* crystal structures in complex with H1 antigen and LNB and site-directed mutagenesis experiments revealed that both glycans bind to the P[8] VP8* protein through a binding pocket shared with other members of the P[II] genogroup (i.e.: P[4], P[6] and P[19]). Our results show that the L-fucose moiety from H1 only displays indirect contacts with P[8] VP8*. However, the induced conformational changes in the LNB moiety increase the ligand affinity by two-fold, as measured by surface plasmon resonance (SPR), providing a molecular explanation for the different susceptibility to rotavirus infection between secretor and non-secretor individuals. The unexpected interaction of P[8] VP8* with LNB, a building block of type-1 human milk oligosaccharides, resulted in inhibition of rotavirus infection, highlighting the role and possible application of this disaccharide as an antiviral. While key amino acids in the H1/LNB binding pocket were highly conserved in members of the P[II] genogroup, differences were found in ligand affinities among distinct P[8] genetic lineages. The variation in affinities were explained by subtle structural differences induced by amino acid changes in the vicinity of the binding pocket, providing a fine-tuning mechanism for glycan binding in P[8] rotavirus. | ||
| - | + | Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens.,Gozalbo-Rovira R, Ciges-Tomas JR, Vila-Vicent S, Buesa J, Santiso-Bellon C, Monedero V, Yebra MJ, Marina A, Rodriguez-Diaz J PLoS Pathog. 2019 Jun 21;15(6):e1007865. doi: 10.1371/journal.ppat.1007865. PMID:31226167<ref>PMID:31226167</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6h9w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Group a rotaviruses]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buesa, J]] | ||
| + | [[Category: Ciges-Tomas, J R]] | ||
| + | [[Category: Gozalbo-Rovira, R]] | ||
| + | [[Category: Marina, A]] | ||
| + | [[Category: Monedero, V]] | ||
| + | [[Category: Rodriguez-Diaz, J]] | ||
| + | [[Category: Santiso-Bellon, C]] | ||
| + | [[Category: Vila-Vicent, S]] | ||
| + | [[Category: Yebra, M J]] | ||
| + | [[Category: Histo-blood group antigen rotavirus]] | ||
| + | [[Category: Viral protein]] | ||
Current revision
Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens
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