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==CryoEM Structure of Foot and Mouth Disease Virus O PanAsia== | |||
<StructureSection load='5ned' size='340' side='right' caption='[[5ned]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ned]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NED FirstGlance]. <br> | |||
</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=5ned FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ned OCA], [http://pdbe.org/5ned PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ned RCSB], [http://www.ebi.ac.uk/pdbsum/5ned PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ned ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally alphavbeta6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between alphavbeta6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role. | |||
Rules of engagement between alphavbeta6 integrin and foot-and-mouth disease virus.,Kotecha A, Wang Q, Dong X, Ilca SL, Ondiviela M, Zihe R, Seago J, Charleston B, Fry EE, Abrescia NGA, Springer TA, Huiskonen JT, Stuart DI Nat Commun. 2017 May 23;8:15408. doi: 10.1038/ncomms15408. PMID:28534487<ref>PMID:28534487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ned" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kotecha, A]] | |||
[[Category: Stuart, D]] | [[Category: Stuart, D]] | ||
[[Category: | [[Category: Fmdv]] | ||
[[Category: Foot and mouth disease virus]] | |||
[[Category: Opanasia]] | |||
[[Category: Virus]] | |||
Revision as of 06:56, 4 August 2017
CryoEM Structure of Foot and Mouth Disease Virus O PanAsiaCryoEM Structure of Foot and Mouth Disease Virus O PanAsia
Structural highlights
Publication Abstract from PubMedFoot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally alphavbeta6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between alphavbeta6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role. Rules of engagement between alphavbeta6 integrin and foot-and-mouth disease virus.,Kotecha A, Wang Q, Dong X, Ilca SL, Ondiviela M, Zihe R, Seago J, Charleston B, Fry EE, Abrescia NGA, Springer TA, Huiskonen JT, Stuart DI Nat Commun. 2017 May 23;8:15408. doi: 10.1038/ncomms15408. PMID:28534487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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