Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus
- Published
- Accepted
- Subject Areas
- Agricultural Science, Biochemistry, Microbiology, Molecular Biology, Virology
- Keywords
- Foot-and-mouth disease virus, crystal structure, 3C protease, proteolytic processing, picornavirus, South African Territories serotype
- Copyright
- © 2016 Yang et al.
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
- Cite this article
- 2016. Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus. PeerJ PrePrints 4:e1750v1 https://doi.org/10.7287/peerj.preprints.1750v1
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 3.2Å resolution of 3Cpro from SAT2/GHA/8/91).
Author Comment
This is a preprint submission to PeerJ.