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. 2009 Mar 13;5(3):e1000339. doi: 10.1371/journal.ppat.1000339

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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(A) Schematic representation of the domain organization of Alix. Bro1: BCK1-like resistance to osmotic shock 1, V: V-shaped domain, PRD: Proline Rich Domain. Numbers indicate positions of amino acid residues. (B) Virus-release assay showing that over-expression of Alix inhibits virus release. 293T cells were transfected with either wild-type (wt) pNL4-3 plasmid alone or with increasing amounts of HA-Alix. Pelleted virions and cell lysates were analyzed by SDS-PAGE and western blot using the indicated antibodies. Gag intermediate products are indicated with (*) symbols. (C) Relative release efficiency of HIV-1 virions upon over-expression of Alix. The release efficiency in presence of Alix (calculated at the highest amount shown in B, lane 4) is relative to the release efficiency of NL4-3 alone, which was arbitrarily set at 100. Error bars indicate the standard deviation from four separate experiments. (D) Transmission Electron Microscopy (TEM) images of thin-sectioned 293T cells transfected with pNL4-3 wt alone (upper left panel) or pNL4-3 wt + Alix (lower left panel and close-ups of regions of interest a, b, c) showing arrested budding particles.