Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus

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 re...

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Bibliographic Details
Published in:PeerJ preprints 2016-02
Main Authors: Yang, Jingjie, Leen, Eoin N, Maree, Francois F, Curry, Stephen
Format: Article
Language:English
Subjects:
Crystal structure
Foot & mouth disease
Genomes
Phylogeny
Proteinase
Proteolysis
Purification
Ribonucleic acid
RNA
RNA viruses
Serotypes
Trypsin
Viruses
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Summary: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).
ISSN:2167-9843
DOI:10.7287/peerj.preprints.1750v1