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Journal of Virology, March 2000, p. 2930-2935, Vol. 74, No. 6
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The SU and TM Envelope Protein Subunits of Bovine Leukemia Virus Are Linked by Disulfide Bonds, both in Cells and in Virions

Elizabeth R. Johnstondagger and Kathryn Radke*

Department of Animal Science and Graduate Group in Biochemistry and Molecular Biology, University of California, Davis, California 95616-8521

Received 30 September 1999/Accepted 8 December 1999

After the polyprotein precursor of retroviral envelope proteins is proteolytically cleaved, the surface (SU) and transmembrane (TM) subunits remain associated with each other by noncovalent interactions or by disulfide bonds. Disulfide linkages confer a relatively stable association between the SU and TM envelope protein subunits of Rous sarcoma virus and murine leukemia virus. In contrast, the noncovalent association between SU and TM of human immunodeficiency virus leads to significant shedding of SU from the surface of infected cells. The SU and TM proteins of bovine leukemia virus (BLV) initially were reported to be disulfide linked but later were concluded not to be, since TM is often lost during purification of SU protein. Here, we show that SU and TM of BLV do, indeed, associate through disulfide bonds, whether the envelope proteins are overexpressed in transfected cells, are produced in virus-infected cells, or are present in newly produced virions.

* Corresponding author. Mailing address: Department of Animal Science, University of California, One Shields Ave., Davis, CA 95616-8521. Phone: (530) 752-9025. Fax: (530) 752-0175. E-mail: KLRadke{at}ucdavis.edu.

dagger Present address: Division of Infectious Diseases, School of Medicine, Stanford University, Stanford, CA 94305-5107.

Journal of Virology, March 2000, p. 2930-2935, Vol. 74, No. 6
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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