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J. Biol. Chem., Vol. 265, Issue 16, 9062-9065, 06, 1990
MG Cordingley, PL Callahan, VV Sardana, VM Garsky and RJ Colonno
A series of synthetic peptides representing authentic proteolytic cleavage
sites of human rhinovirus type 14 were assayed as substrates for purified
3C protease. Competition cleavage assays were employed to determine the
relative specificity constants (Kcat/Km) for substrates with sequences
related to the viral 2C-3A cleavage site. Variable length peptides
representing the 2C-3A cleavage site were cleaved with comparable
efficiency. These studies defined a minimum substrate of 6 amino acids
(TLFQ/GP), although retention of the residue at position P5 (ETLFQ/GP)
resulted in a better substrate by an order of magnitude. Amino acid
substitutions at position P5, P4, P1', or P2' indicated that the identity
of the residue at position P5 was not critical, whereas substitutions at
position P4, P1' or P2' resulted in substrates with Kcat/Km values varying
over 2 orders of magnitude. In contrast to the 2C-3A cleavage site, small
peptide derivatives representative of the 3A- 3B cleavage site were
relatively poor substrates, which suggested that residues flanking the
minimum core sequence may influence susceptibility to cleavage. The 3C
protease of rhinovirus type 14 was also capable of cleaving peptides
representing comparable cleavage sites predicted for coxsackie B virus and
poliovirus.
Substrate requirements of human rhinovirus 3C protease for peptide cleavage in vitro
Department of Virus and Cell Biology, Merck Sharp and Dohme Research Laboratories, West Point, Pennsylvania 19486.
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