Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus
File(s)
Published version
Author(s)
Yang, J
Leen, EN
Maree, FF
Curry, S
Type
Report
Abstract
The replication of foot-and-mouth disease virus (FMDV) is dependent on the virus-encoded 3C protease (3Cpro). As in other picornaviruses, 3Cpro performs most of the proteolytic processing of the polyprotein expressed from the single open reading frame in the RNA genome of the virus. Previous work revealed that the 3Cpro from serotype A – one of the seven serotypes of FMDV – adopts a trypsin-like fold. Phylogenetically the FMDV serotypes are grouped into two clusters, with O, A, C, and Asia 1 in one, and the three South African Territories serotypes, (SAT-1, SAT-2 and SAT-3) in another. We report here the cloning, expression and purification of 3C proteases from four SAT serotype viruses (SAT2/GHA/8/91, SAT1/NIG/5/81, SAT1/UGA/1/97, and SAT2/ZIM/7/83) and the crystal structure at 3.2 Å resolution of 3Cpro from SAT2/GHA/8/91).
Date Issued
2016-02-16
Citation
PeerJ Preprints, 2016, pp.1-18
Publisher
PeerJ Preprints
Start Page
1
End Page
18
Journal / Book Title
PeerJ Preprints
Copyright Statement
© 2016 The Authors. This is a preprint submission to PeerJ
Sponsor
Wellcome Trust
Identifier
http://www.imperial.ac.uk/people/s.curry
Grant Number
083248/Z/07/Z
Subjects
Foot-and-mouth disease virus
Crystal structure
3C protease
Proteolytic processing
Picornavirus
Notes
Published as a preprint; submitted to PeerJ for peer review (on 15 Feb 2016). Decision awaited
Publication Status
Published