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

PeerJ

article

Jingjie Yang¹  Eoin N. Leen¹  Francois F. Maree²  Stephen Curry¹ 

[1] Department of Life Sciences, Imperial College;Transboundary Animal Disease Programme, Agricultural Research Council, Onderstepoort Veterinary Institute

关键词: Foot-and-mouth disease virus;    Crystal structure;    3C protease;    Proteolytic processing;    Picornavirus;    Southern African Territories serotype;   

DOI  :  10.7717/peerj.1964

学科分类：社会科学、人文和艺术（综合）

来源: Inra

【 摘 要 】

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 large 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. On the basis of capsid sequence comparisons the FMDV serotypes are grouped into two phylogenetic clusters, with O, A, C, and Asia 1 in one, and the three Southern African Territories serotypes, (SAT-1, SAT-2 and SAT-3) in another, a grouping pattern that is broadly, but not rigidly, reflected in 3Cpro amino acid sequences. 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.

【 授权许可】

CC BY