Identification and characterization of Iflavirus 3C-like protease processing activities

Shan Ye, Hongjie Xia, Chen Dong, Zhenyun Cheng, Xiaoling Xia, Jiamin Zhang, Xi Zhou, Yuanyang Hu

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Viral replication and capsid assembly in the viruses in the order . Picornavirales requires polyprotein proteolytic processing by 3C or 3C-like (3CL) proteases. We identified and characterized the 3CL protease of . Ectropis obliqua virus (EoV) of the newly established family . Iflaviridae (order . Picornavirales). The bacterially expressed EoV 3CL protease domain autocatalytically released itself from larger precursors by proteolytic cleavage, and cleavage sites were determined via N-terminal sequencing of the cleavage products. This protease also mediated . trans-proteolytic activity and cleaved the polyprotein at the same specific positions. Moreover, we determined the critical catalytic residues (H2261, D2299, C2383) for the protease activity, and characterized the biochemical properties of EoV 3CL and its responses to various protease inhibitors. Our work is the first study to identify an iflaviral 3CL protease and further characterize it in detail and should foster our understanding of EoV and other iflaviruses.

Original languageEnglish (US)
Pages (from-to)136-145
Number of pages10
JournalVirology
Volume428
Issue number2
DOIs
StatePublished - Jul 5 2012
Externally publishedYes

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Keywords

  • 3C-like protease
  • Autocatalytic polyprotein processing
  • Cleavage sites
  • Ectropis obliqua virus
  • Iflavirus
  • Picornavirales
  • Trans cleavage

ASJC Scopus subject areas

  • Virology

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