| Status: waiting for Mol* initialization | |
|
Structural highlights
Function
Q98W00_FMDVO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Rules of engagement between alphavbeta6 integrin and foot-and-mouth disease virus. Nat Commun. 2017 May 23;8:15408. doi: 10.1038/ncomms15408. PMID:28534487 doi:https://dx.doi.org/10.1038/ncomms15408
|
