What question did this study set out to answer?

To determine whether and how the HIV-1 structural precursor polyprotein Pr55 Gag interacts with the host ubiquitin-related protein Tsg101 to mediate viral particle release.

June 26, 2001Proceedings of the National Academy of SciencesOpen Access

Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag

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Authors

LVLynn VerPlankBroad Institute FBFadila BouamrNational Institutes of Health TLTracy J. LaGrassaOsnabrück University

Discussion

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Implication

Laboratory study demonstrates that Tsg101 binds the HIV-1 Pr55 Gag late domain, indicating a direct link between viral particle release and host trafficking machinery.

Key Points

To determine whether and how the HIV-1 structural precursor polyprotein Pr55 Gag interacts with the host ubiquitin-related protein Tsg101 to mediate viral particle release.
Evaluated protein-protein interactions using a yeast two-hybrid system.
Performed in vitro coimmunoprecipitation assays using purified Pr55 Gag and rabbit reticulocyte lysate-synthesized Tsg101.
Analyzed in vivo binding in gag-transfected COS cells alongside site-directed mutagenesis targeting Tsg101 and the Gag p6 region.
Tsg101 specifically bound the PTAPP late (L) domain within the p6 region of Pr55 Gag in yeast, cell-free, and mammalian cell systems.
Binding was mediated by the N-terminal domain of Tsg101, which is structurally homologous to Ubc4-class ubiquitin-conjugating (E2) enzymes.
Mutating Tyr-110, an active-site variant distinguishing Tsg101 from active E2 enzymes, impaired binding to the viral p6 domain.

Cite This Study

VerPlank et al. (2001) studied this question.

synapsesocial.com/papers/6a731e0ff422c06c4f2b3116 https://doi.org/10.1073/pnas.131059198

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June 26, 2001Proceedings of the National Academy of SciencesOpen Access

Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag

View Full Paper

Ask AI

Bookmark

Authors

LVLynn VerPlankBroad Institute FBFadila BouamrNational Institutes of Health TLTracy J. LaGrassaOsnabrück University

Discussion

Member takes

Implication

Laboratory study demonstrates that Tsg101 binds the HIV-1 Pr55 Gag late domain, indicating a direct link between viral particle release and host trafficking machinery.

Key Points

To determine whether and how the HIV-1 structural precursor polyprotein Pr55 Gag interacts with the host ubiquitin-related protein Tsg101 to mediate viral particle release.
Evaluated protein-protein interactions using a yeast two-hybrid system.
Performed in vitro coimmunoprecipitation assays using purified Pr55 Gag and rabbit reticulocyte lysate-synthesized Tsg101.
Analyzed in vivo binding in gag-transfected COS cells alongside site-directed mutagenesis targeting Tsg101 and the Gag p6 region.
Tsg101 specifically bound the PTAPP late (L) domain within the p6 region of Pr55 Gag in yeast, cell-free, and mammalian cell systems.
Binding was mediated by the N-terminal domain of Tsg101, which is structurally homologous to Ubc4-class ubiquitin-conjugating (E2) enzymes.
Mutating Tyr-110, an active-site variant distinguishing Tsg101 from active E2 enzymes, impaired binding to the viral p6 domain.

Cite This Study

VerPlank et al. (2001) studied this question.

synapsesocial.com/papers/6a731e0ff422c06c4f2b3116 https://doi.org/10.1073/pnas.131059198

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