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Originally published In Press as doi:10.1074/jbc.M006844200 on October 12, 2000

J. Biol. Chem., Vol. 276, Issue 1, 780-787, January 5, 2001
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African Swine Fever Virus Protease, a New Viral Member of the SUMO-1-specific Protease Family*

Germán AndrésDagger §, Alí AlejoDagger , Carmen Simón-Mateo, and María L. Salas||

From the Centro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain

African swine fever virus (ASFV) is a complex DNA virus that employs polyprotein processing at Gly-Gly-Xaa sites as a strategy to produce several major core components of the viral particle. The virus gene S273R encodes a 31-kDa protein that contains a "core domain" with the conserved catalytic residues characteristic of SUMO-1-specific proteases and the adenovirus protease. Using a COS cell expression system, it was found that protein pS273R is capable of cleaving the viral polyproteins pp62 and pp220 in a specific way giving rise to the same intermediates and mature products as those produced in ASFV-infected cells. Furthermore, protein pS273R, like adenovirus protease and SUMO-1-specific enzymes, is a cysteine protease, because its activity is abolished by mutation of the predicted catalytic histidine and cysteine residues and is inhibited by sulfhydryl-blocking reagents. Protein pS273R is expressed late after infection and is localized in the cytoplasmic viral factories, where it is found associated with virus precursors and mature virions. In the virions, the protein is present in the core shell, a domain where the products of the viral polyproteins are also located. The identification of the ASFV protease will allow a better understanding of the role of polyprotein processing in virus assembly and may contribute to our knowledge of the emerging family of SUMO-1-specific proteases.

* This work was supported by Dirección General de Investigación Científica y Técnica Grant PB96-0902-C02-01, European Community Grant FAIR5-CT97-3441, Ministerio de Educación y Cultura Grant AGF98-1352-CE, and an institutional grant from the Fundación Ramón Areces.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger The first two authors contributed equally to this work.

§ Fellow of the Comunidad Autónoma de Madrid.

Present address: Centro Nacional de Biotecnología (CSIC), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain.

|| To whom correspondence should be addressed: Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain. Tel.: 34-913978478; Fax: 34-913974799; E-mail: mlsalas@cbm.uam.es.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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