Sequential autoprocessing of Marek's disease herpesvirus protease differs from that of other herpesviruses.
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.
Laurent
S
S
Equipe Télomérase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, INRA de Tours, 37380 Nouzilly, France. slaurent@tours.inra.fr
Blondeau
C
C
Belghazi
M
M
Remy
S
S
Esnault
E
E
Rasschaert
P
P
Rasschaert
D
D
D000818:Animals; D001665:Binding Sites; D008381:Herpesvirus 2, Gallid / Q000201:enzymology*; D006868:Hydrolysis; D008380:Marek Disease / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000096:biosynthesis / Q000378:metabolism*; D020815:Polyproteins / Q000096:biosynthesis / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D020815:Polyproteins; D010447:Peptide Hydrolases