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Journal of Virology, June 2000, p. 5373-5376, Vol. 74, No. 11
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Ubiquitination of the Human Immunodeficiency Virus Type 1 Env Glycoprotein

Andreas Bültmann, Josef Eberle, and Jürgen Haas*

Max-von-Pettenkofer Institut, Genzentrum, LMU München, 81377 Munich, Germany

Received 12 October 1999/Accepted 7 March 2000

Expression of the human immunodeficiency virus type 1 (HIV-1) Env glycoprotein is stringently regulated in infected cells. The majority of the glycoprotein does not reach the cell surface but rather is retained in the endoplasmic reticulum or a cis-Golgi compartment and subsequently degraded. We here report that Env of various HIV-1 isolates is ubiquitinated at the extracellular domain of gp41 and that Env expression could be increased by lactacystin, a specific proteasome inhibitor, suggesting that the ubiquitin/proteasome system is involved in control of expression and degradation.

* Corresponding author. Mailing address: Max-von-Pettenkofer Institut, Genzentrum, LMU München, Feodor-Lynen-Str. 25, 81377 Munich, Germany. Phone: 49 89 2180 6852. Fax: 49 89 2180 6899. E-mail: haas{at}lmb.uni-muenchen.de.

Journal of Virology, June 2000, p. 5373-5376, Vol. 74, No. 11
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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