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. 1991 Jun;182(2):861-4.
doi: 10.1016/0042-6822(91)90630-t.

Autoproteolytic cleavage of recombinant 3C proteinase of hepatitis A virus

V Gauss-Müller  1 , D Jürgensen, R Deutzmann
Affiliations

Autoproteolytic cleavage of recombinant 3C proteinase of hepatitis A virus

V Gauss-Müller et al. Virology. 1991 Jun.

Abstract

A hepatitis A virus cDNA fragment coding for the viral proteinase 3C was expressed as a chimeric protein fused in-frame to the C-terminus of beta-galactosidase. Following induction of the lac Z promoter, polypeptides of 150, 28, 26, and 16 kDa, all of which carry 3C antigenicity, were produced. The 28- and 26-kDa proteins were identified as autoproteolytic products of the fusion protein by determination of their N-terminal amino acid sequence. The 16-kDa protein arises from internal initiation. Following substitution of the 37 amino acids at the C-terminus of 3C, the autolytic activity was no longer observed. The recombinant proteinase did not show trans-activity when recombinant proteins of the P1 or P2 region were used as substrates. Antisera directed against recombinant 3C could not detect 3C or its precursors in HAV-infected cells.

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