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Sequential autoprocessing of Marek's disease herpesvirus protease differs from that of other herpesviruses

S Laurent1, C Blondeau, M Belghazi

  • 1Equipe Télomérase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, INRA de Tours, 37380 Nouzilly, France. slaurent@tours.inra.fr

Journal of Virology
|March 23, 2007
PubMed

Insights

Marek's disease virus protease autoprocessing was studied. The atypical M site cleavage by the short protease makes this herpesvirus unique.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Herpesviruses possess a unique serine protease crucial for viral capsid maturation.
  • This protease undergoes autoprocessing at specific cleavage sites.

Purpose of the Study:

  • To investigate the autoprocessing of Marek's disease virus (MDV) protease.
  • To elucidate the cleavage mechanism at the R and M sites, particularly the non-consensus M site.

Main Methods:

  • Production of MDV protease polyprotein in Escherichia coli.
  • Site-directed mutagenesis to confirm and alter cleavage site sequences.
  • Expression kinetics studies to analyze protease activity.

Main Results:

  • Complete autoprocessing of MDV protease at both R and M sites was observed.
  • The M site was confirmed to have a non-consensus sequence (M(P3)-N(P2)-A(P1)/S(P1')).
  • Mutagenesis and expression kinetics indicated exclusive cleavage of the M site by the processed short protease.

Conclusions:

  • The MDV protease autoprocessing mechanism, especially at the M site, is unique among herpesviruses.
  • The atypical M site cleavage by the short protease is a distinguishing feature of MDV.
  • This finding provides insights into the specific molecular mechanisms of MDV replication and maturation.

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