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