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Maturation of the polymerase polyprotein of the coronavirus MHV strain JHM involves a cascade of proteolytic

J J Schiller1, S C Baker

  • 1Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, Illinois 60153, USA.

Advances in Experimental Medicine and Biology
|October 23, 1998
PubMed

Insights

Researchers identified viral proteins produced by the mouse hepatitis virus (MHV) polymerase. They pinpointed specific viral proteinase domains responsible for generating these MHV proteins, aiding in understanding coronavirus replication.

Area of Science:

  • Virology
  • Molecular Biology
  • Coronaviridae

Background:

  • Murine coronavirus mouse hepatitis virus (MHV) RNA polymerase gene encodes a large polyprotein (>750 kDa).
  • The amino-terminal cleavage product, p28, is processed by the viral protease PCP-1.

Purpose of the Study:

  • To identify proteolytic products downstream of p28 in MHV-JHM.
  • To determine the viral proteinase domains responsible for generating these products.

Main Methods:

  • Generation of antisera against specific MHV-JHM ORF1a regions.
  • Identification of viral proteins in MHV-JHM-infected cells using these antisera.

Main Results:

  • Six viral proteins were identified, representing a significant portion of ORF1a.
  • Identified proteins include p28, p72, p65, p250, p210, and p27.

Conclusions:

  • The study successfully identified key proteolytic products of the MHV-JHM polymerase polyprotein.
  • This work contributes to understanding the processing and function of viral proteases in coronavirus replication.

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