期刊
NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms15408
关键词
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资金
- Wellcome Trust [060208/Z/00/Z, 093305/Z/10/Z, 090532/Z/09/Z]
- Spanish Ministerio de Economia y Competitividad [BFU2015-64541-R]
- European Research Council under the European Union [649053]
- Chinese Academy of Sciences
- UK MRC [G1000099, G1100525/1, MR/N00065X/1]
- European Research Council (ERC) [649053] Funding Source: European Research Council (ERC)
- Biotechnology and Biological Sciences Research Council [BBS/E/I/00007030, BBS/E/I/00001715, BBS/E/I/00001494] Funding Source: researchfish
- BBSRC [BBS/E/I/00001715, BBS/E/I/00007030, BBS/E/I/00001494] Funding Source: UKRI
- MRC [MR/N00065X/1] Funding Source: UKRI
Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally alpha v beta 6, 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 alpha v beta 6 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.
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