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Coronaviruses pp 227-232 | Cite as

Proteolytic Processing of the N-terminal Region of the Equine Arteritis Virus Replicase

  • Eric J. Snijder
  • Alfred L. M. Wassenaar
  • Willy J. M. Spaan
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 342)

Abstract

A papainlike cysteine protease (PCP) domain in the N-terminal region of the equine arteritis virus (EAV) replicase was identified by in vitro translation and mutagenesis studies. The EAV protease was found to direct an autoproteolytic cleavage at its C-terminus which leads to the production of an approximately 30K N-terminal replicase product (nspl) containing the PCP domain. Amino acid residues Cys164 and His230 of the EAV replicase polyprotein were identified as the most likely candidates for the role of PCP catalytic residues. It was sshown that cleavage occurs in cis between Gly260 and Gly261

Keywords

Cleavage Product Active Site Residue Protease Domain Rabbit Reticulocyte Lysate Equine Arteritis Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Eric J. Snijder
    • 1
  • Alfred L. M. Wassenaar
    • 1
  • Willy J. M. Spaan
    • 1
  1. 1.Department of Virology, Institute of Medical Microbiology Faculty of MedicineLeiden UniversityLeidenThe Netherlands

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