Putative Papain-related Thiol Proteases of Positive-strand RNA Viruses. Identification of Rubi- and Aphthovirus Proteases and Delineation of a Novel Conserved Domain Associated with Proteases of Rubi-, Alpha- and Coronaviruses

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 1991 Aug 19

PMID 1652473

Citations 176

Authors

A E Gorbalenya

E V Koonin

M M Lai

Affiliations

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Abstract

A computer-assisted comparative analysis of the amino acid sequences of (putative) thiol proteases encoded by the genomes of several diverse groups of positive-stranded RNA viruses and distantly related to the family of cellular papain-like proteases is presented. A high level of similarity was detected between the leader protease of foot-and-mouth-disease virus and the protease of murine hepatitis coronavirus which cleaves the N-terminal p28 protein from the polyprotein. Statistically significant alignment of a portion of the rubella virus polyprotein with cellular papain-like proteases was obtained, leading to tentative identification of the papain-like protease as the enzyme mediating processing of the non-structural proteins of this virus. Specific grouping between the sequences of the proteases of alpha-viruses, and poty- and bymoviruses was revealed. It was noted that papain-like proteases of positive-stranded RNA viruses are much more variable both in their sequences and in genomic locations than chymotrypsin-related proteases found in the same virus class. A novel conserved domain of unknown function has also been identified which flanks the papain-like proteases of alpha-, rubi- and coronaviruses.

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