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Journal of Virology, June 2007, p. 6117-6121, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.02679-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Sequential Autoprocessing of Marek's Disease Herpesvirus Protease Differs from That of Other Herpesviruses{triangledown}

S. Laurent,1* C. Blondeau,1 M. Belghazi,3 S. Remy,1 E. Esnault,1 P. Rasschaert,1 and D. Rasschaert1,2

Equipe Télomérase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, INRA de Tours, 37380 Nouzilly, France,1 UFR Sciences et Techniques de l'Université François Rabelais de Tours, 37200 Tours, France,2 Service de Spectrométrie de Masse pour la protéomique, Unité PRC, INRA de Tours, 37380 Nouzilly, France3

Received 5 December 2006/ Accepted 14 March 2007

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.

* Corresponding author. Mailing address: Equipe Télomérase et Lymphome Viro-induit, UPR INRA 1282 IASP-213, INRA de Tours, 37380 Nouzilly, France. Phone: 33 247427682. Fax: 33 247427774. E-mail: slaurent{at}tours.inra.fr

{triangledown} Published ahead of print on 21 March 2007.

Journal of Virology, June 2007, p. 6117-6121, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.02679-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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