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Rules of engagement between αvβ6 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 8 15408 (2017)
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Cited: 47 times
EuropePMC logo PMID: 28534487

Abstract

Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally αvβ6, 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 αvβ6 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.

Articles - 5nem mentioned but not cited (2)

  1. Rules of engagement between αvβ6 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 8 15408 (2017)
  2. Structures of Foot-and-Mouth Disease Virus with Bovine Neutralizing Antibodies Reveal the Determinant of Intraserotype Cross-Neutralization. He Y, Li K, Wang L, Sun Z, Cao Y, Li P, Sun P, Bao H, Zhou S, Wang S, Bai X, Liu X, Zhao L, Fan X, Liu Z, Lu Z, Yang C, Lou Z. J Virol 95 e0130821 (2021)


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