Accueil > Bibliographie > Sequential autoprocessing of Marek’s disease herpesvirus protease differs (...)

Sequential autoprocessing of Marek’s disease herpesvirus (...)

J Virol. 2007 Jun ;81(11):6117-21
Sequential autoprocessing of Marek’s disease herpesvirus protease differs from that of other herpesviruses.
Laurent S, Blondeau C, Belghazi M, Remy S, Esnault E, Rasschaert P, Rasschaert D.

Herpesviruses encode a unique serine protease essential for viral capsid maturation. This protease undergoes autoprocessing at two sites, R and M, at the consensus sequence (V, L, I)(P3)-X(P2)-A(P1)/S(P1’) (where X is a polar amino acid). We observed complete autoprocessing at the R and M sites of Marek’s disease virus (MDV) protease following production of the polyprotein in Escherichia coli. Site-directed mutagenesis confirmed the predicted sequence of the R and M sites, with the M site sequence being nonconsensual : M(P3)-N(P2)-A(P1)/S(P1’). Mutagenesis and expression kinetics studies suggested that the atypical MDV M site was cleaved exclusively by the processed short protease, a feature making MDV unique among herpesviruses.

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