Ontology highlight
ABSTRACT:
SUBMITTER: Oka T
PROVIDER: S-EPMC1933329 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Oka Tomoichiro T Yamamoto Mami M Yokoyama Masaru M Ogawa Satoko S Hansman Grant S GS Katayama Kazuhiko K Miyashita Kana K Takagi Hirotaka H Tohya Yukinobu Y Sato Hironori H Takeda Naokazu N
Journal of virology 20070425 13
A common feature of caliciviruses is the proteolytic processing of the viral polyprotein catalyzed by the viral 3C-like protease encoded in open reading frame 1 (ORF1). Here we report the identification and structural characterization of the protease domains and amino acid residues in sapovirus (SaV) and feline calicivirus (FCV). The in vitro expression and processing of a panel of truncated ORF1 polyproteins and corresponding mutant forms showed that the functional protease domain is 146 amino ...[more]