Sequential autoprocessing of Marek's disease herpesvirus protease differs from that of other herpesviruses |
| |
| Authors: | Laurent S Blondeau C Belghazi M Remy S Esnault E Rasschaert P Rasschaert D |
| |
| Affiliation: | Equipe Télomérase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, INRA de Tours, 37380 Nouzilly, France. slaurent@tours.inra.fr |
| |
| Abstract: | 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. |
| |
| Keywords: | |
| 本文献已被 PubMed 等数据库收录！ |
|
