Marek's disease virus; serine protease; R and M sites
Abstract :
[en] 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-XP2-AP1/SP1' (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: MP3-NP2-AP1/SP1'. 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.
Disciplines :
Life sciences: Multidisciplinary, general & others
Author, co-author :
Laurent, Sylvie; Institut Scientifique de Recherche Agronomique - INRA > sante animale > Equipe Telomerase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, Nouzilly
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