Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus

Abhay Kotecha, Quan Wang, Xianchi Dong, Serban L. Ilca, Marina Ondiviela, Rao Zihe, Julian Seago, Bryan Charleston, Elizabeth E. Fry, Nicola G. A. Abrescia, Timothy A. Springer (), Juha T. Huiskonen () and David I. Stuart ()
Additional contact information
Abhay Kotecha: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Quan Wang: National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences
Xianchi Dong: Boston Children's Hospital
Serban L. Ilca: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Marina Ondiviela: Structural Biology Unit, CIC bioGUNE, CIBERehd
Rao Zihe: National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences
Julian Seago: Pirbright Institute
Bryan Charleston: Pirbright Institute
Elizabeth E. Fry: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Nicola G. A. Abrescia: Structural Biology Unit, CIC bioGUNE, CIBERehd
Timothy A. Springer: Boston Children's Hospital
Juha T. Huiskonen: University of Oxford, The Henry Wellcome Building for Genomic Medicine
David I. Stuart: University of Oxford, The Henry Wellcome Building for Genomic Medicine

Nature Communications, 2017, vol. 8, issue 1, 1-8

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms15408 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15408

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms15408

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().