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Reference: Kotecha, A, Wang, Q, Dong, X et al., (2017). Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus. Nature Communications, 8, 15408.Citable link to this page:

 

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

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.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionDate of acceptance:2017-03-26 Funder: Wellcome Trust   Funder: Spanish Ministry of Economy, Industry and Competitiveness   Funder: Horizon 2020   Funder: Chinese Academy of Sciences   Funder: Medical Research Council   Notes:© The Author(s) 2017. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

Bibliographic Details

Publisher: Nature Publications

Publisher Website: http://www.nature.com/

Journal: Nature Communicationssee more from them

Publication Website: http://www.nature.com/ncomms/index.html

Volume: 8

Issue Date: 2017-05

pages:15408Identifiers

Doi: https://doi.org/10.1038/ncomms15408

Eissn: 2041-1723

Uuid: uuid:2eb40ba4-fb39-4852-b58a-233597467655

Urn: uri:2eb40ba4-fb39-4852-b58a-233597467655

Pubs-id: pubs:697017 Item Description

Type: journal-article;

Language: eng

Version: Publisher's versionKeywords: Journal Article

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Author: Kotecha, A - Oxford, MSD, NDM, Structural Biology - - - Wang, Q - - - Dong, X - - - Ilca, SL - Oxford, MSD, Doctoral Training Cen

Source: https://ora.ox.ac.uk/objects/uuid:2eb40ba4-fb39-4852-b58a-233597467655



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