Abstract
The Nef protein enhances human immunodeficiency virus type 1 (HIV-1) infectivity by facilitating an early postentry step in the virus life cycle. We report here that the addition of MG132 or lactacystin, each a specific inhibitor of cellular proteasome activity, preferentially enhances cellular permissiveness to infection by Nef-defective versus wild-type HIV-1. Pseudotyping by the glycoprotein of vesicular stomatitis virus rendered Nef-defective HIV-1 particles minimally responsive to the enhancing effects of proteasome inhibitors. These results suggest that Nef enhances the infectivity of HIV-1 particles by reducing their susceptibility to proteasomal degradation in target cells.
Highlights
Encoded by primate lentiviruses, the accessory protein Nef promotes human immunodeficiency virus type 1 (HIV-1) infection by a poorly defined mechanism
Pseudotyping by the glycoprotein of vesicular stomatitis virus rendered Nef-defective HIV-1 particles minimally responsive to the enhancing effects of proteasome inhibitors. These results suggest that Nef enhances the infectivity of HIV-1 particles by reducing their susceptibility to proteasomal degradation in target cells
Despite the lack of an apparent effect of Nef on HIV-1 entry, the requirement for Nef in HIV-1 infection can be markedly reduced by the pseudotyping of HIV-1 cores by the glycoproteins of heterologous enveloped viruses that depend on endosomal acidification for fusion [1, 7, 14]
Summary
Encoded by primate lentiviruses, the accessory protein Nef promotes human immunodeficiency virus type 1 (HIV-1) infection by a poorly defined mechanism. We report here that the addition of MG132 or lactacystin, each a specific inhibitor of cellular proteasome activity, preferentially enhances cellular permissiveness to infection by Nefdefective versus wild-type HIV-1. Pseudotyping by the glycoprotein of vesicular stomatitis virus rendered Nef-defective HIV-1 particles minimally responsive to the enhancing effects of proteasome inhibitors.
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