Table 1.

Relative rates of cleavage of HCV 229E 3CLp r opeptide substrates

Cleavage siteaPeptideSequenceb(Vmax/Km )relc
P8P7P6P5P4P3P2P1P1′P2′P3′P4′P5′P6′P7′
MP1/3CLp r o SP1VSYGSTLQAGLRKMA1.00
3CLp r o/MP2SP4QMFGVNLQSGKTTSM1.17
p23/p12SP5CERVVKLQNNEIMPG0.09
p12/p16SP6IGATVRLQAGKQTEF0.51
  • a MP1, putative membrane protein 1 (10, 13, 20); 3CLpro, 3C-like proteinase (44, 45); MP2, putative membrane protein 2 (10, 13,20); p23, ORF 1a-encoded, 23-kDa processing product (this study); p12, ORF 1a-encoded, 12-kDa processing product (this study); p16, ORF 1a-encoded, 16-kDa processing product (this study).

  • b Amino acids flanking the proteinase cleavage sites are designated according to the scheme introduced by Schechter and Berger (36). The residues are numbered toward the carboxyl terminus as follows: P3-P2-P1↓P1′-P2′-P3′.

  • c RelativeV max/Km values were determined by using competition experiments as described in Materials and Methods with SP1 as the reference peptide.