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J Virol, April 1998, p. 2962-2968, Vol. 72, No. 4
AIDS Vaccine Program,
Received 28 August 1997/Accepted 12 January 1998
Host proteins are incorporated into retroviral virions during
assembly and budding. We have examined three retroviruses, human immunodeficiency virus type 1 (HIV-1), simian immunodeficiency virus
(SIV), and Moloney murine leukemia virus (Mo-MuLV), for the presence of
ubiquitin inside each of these virions. After a protease treatment to
remove exterior viral as well as contaminating cellular proteins, the
proteins remaining inside the virion were analyzed. The results
presented here show that all three virions incorporate ubiquitin
molecules at approximately 10% of the level of Gag found in virions.
In addition to free ubiquitin, covalent ubiquitin-Gag complexes were
detected, isolated, and characterized from all three viruses. Our
immunoblot and protein sequencing results on treated virions showed
that approximately 2% of either HIV-1 or SIV p6Gag was
covalently attached to a single ubiquitin molecule inside the
respective virions and that approximately 2 to 5% of the
p12Gag in Mo-MuLV virions was monoubiquitinated. These
results show that ubiquitination of Gag is conserved among these
retroviruses and occurs in the p6Gag portion of the Gag
polyprotein, a region that is likely to be involved in assembly and
budding.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Ubiquitin Is Covalently Attached to the p6Gag
Proteins of Human Immunodeficiency Virus Type 1 and Simian
Immunodeficiency Virus and to the p12Gag Protein of
Moloney Murine Leukemia Virus

*
Corresponding author. Mailing address: AIDS Vaccine
Program, SAIC/Frederick, Frederick Cancer Research and Development
Center, P.O. Box B, Frederick, MD 21702-1201. Phone: (301) 846-5723. Fax: (301) 846-5588. E-mail: ott{at}avpvx1.ncifcrf.gov.
Present address: Microbiological Research Institute, Otsuka
Pharmaceutical Co., Kawauchi, Tokushima 771-01, Japan.
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