Molecular and Enzymatic Characterization of the Porcine Endogenous Retrovirus Protease

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2002 Jul 5

PMID 12097607

Citations 2

Authors

Jurgen H Blusch

Sigrid Seelmeir

Klaus von der Helm

Affiliations

Soon will be listed here.

Abstract

The protease of the porcine endogenous retrovirus (PERV) subtypes A/B and C was recombinantly expressed in Escherichia coli as proteolytically active enzyme and characterized. The PERV Gag precursor was also recombinantly produced and used as the substrate in an in vitro enzyme assay in parallel with synthetic nonapeptide substrates designed according to cleavage site sequences identified in the PERV Gag precursor. The proteases of all PERV subtypes consist of 127 amino acid residues with an M(r) of 14,000 as revealed by determining the protease N and C termini. The PERV proteases have a high specificity for PERV substrates and do not cleave human immunodeficiency virus (HIV)-specific substrates, nor are they inhibited by specific HIV protease inhibitors. Among the known retroviral proteases, the PERV proteases resemble most closely the protease of the murine leukemia retrovirus.

Citing Articles

Porcine Endogenous Retrovirus (PERV) - Molecular Structure and Replication Strategy in the Context of Retroviral Infection Risk of Human Cells.

Lopata K, Wojdas E, Nowak R, Lopata P, Mazurek U Front Microbiol. 2018; 9:730.

PMID: 29755422 PMC: 5932395. DOI: 10.3389/fmicb.2018.00730.

Characterization of two porcine endogenous retrovirus integration loci and variability in pigs.

Gorbovitskaia M, Liu Z, Bourgeaux N, Li N, Lian Z, Chardon P Immunogenetics. 2003; 55(4):262-70.

PMID: 12827326 DOI: 10.1007/s00251-003-0579-4.

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