Proteolytic processing of the N-terminal region of the equine arteritis virus replicase.
A papainlike cysteine protease (PCP) domain in the N-terminal region of the equine arteritis virus (EAV) replicase was identified by in vitro translation and mutagenesis studies. The EAV protease was found to direct an autoproteolytic cleavage at its C-terminus which leads to the production of an approximately 30K N-terminal replicase product (nsp1) containing the PCP domain. Amino acid residues Cys164 and His230 of the EAV replicase polyprotein were identified as the most likely candidates for the role of PCP catalytic residues. It was shown that cleavage occurs in cis between Gly260 and Gly261.
Snijder
E J
EJ
Department of Virology, Faculty of Medicine, Leiden University, The Netherlands.
Wassenaar
A L
AL
Spaan
W J
WJ
D000595:Amino Acid Sequence; D001483:Base Sequence; D007240:Equartevirus / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017385:Sequence Homology; D014764:Viral Proteins / Q000378:metabolism*
D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; C087637:gene 1 protein, Coronavirus