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Tsg101 and the Vacuolar Protein Sorting Pathway Are Essential for HIV-1 Budding
Jennifer E. Garrus ,
Uta K. von Schwedler ,
Owen W. Pornillos ,
Scott G. Morham ,
Kenton H. Zavitz ,
Hubert E. Wang ,
Daniel A. Wettstein ,
Kirsten M. Stray ,
Mélanie Côté ,
Rebecca L. Rich ,
David G. Myszka ,
Wesley I. Sundquist
October 2001
October 2001
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Abstract
Like other enveloped viruses, HIV-1 uses cellular machinery to bud from infected cells.
We now show that Tsg101 protein, which functions in vacuolar protein sorting (Vps),
is required for HIV-1 budding. The UEV domain of Tsg101 binds to an essential tetrapeptide
(PTAP) motif within the p6 domain of the structural Gag protein and also to ubiquitin.
Depletion of cellular Tsg101 by small interfering RNA arrests HIV-1 budding at a late
stage, and budding is rescued by reintroduction of Tsg101. Dominant negative mutant
Vps4 proteins that inhibit vacuolar protein sorting also arrest HIV-1 and MLV budding.
These observations suggest that retroviruses bud by appropriating cellular machinery
normally used in the Vps pathway to form multivesicular bodies.