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Journal of Virology, February 2007, p. 1502-1505, Vol. 81, No. 3
0022-538X/07/$08.00+0 doi:10.1128/JVI.01711-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Institute of Microbiology, University Hospital of Lausanne, Lausanne, Switzerland,1 Multidisciplinary Oncology Center, University Hospital of Lausanne, Lausanne, Switzerland,2 Ludwig Institute for Cancer Research, Lausanne Branch, Lausanne, Switzerland,3 Swiss Institute of Bioinformatics, Epalinges, Switzerland4
Received 8 August 2006/ Accepted 2 November 2006
The human immunodeficiency virus type 1 (HIV-1) Vpu protein interacts with CD4 within the endoplasmic reticula of infected cells and targets CD4 for degradation through interaction with ß-TrCP1. Mammals possess a homologue of ß-TrCP1, HOS, which is also named ß-TrCP2. We show by coimmunoprecipitation experiments that ß-TrCP2 binds Vpu and is able to induce CD4 down-modulation as efficiently as ß-TrCP1. In two different cell lines, HeLa CD4+ and Jurkat, Vpu-mediated CD4 down-modulation could not be reversed through the individual silencing of endogenous ß-TrCP1 or ß-TrCP2 but instead required the two genes to be silenced simultaneously.
Published ahead of print on 22 November 2006.
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