2014年7月1日
Small molecules that inhibit Vif-induced degradation of APOBEC3G
Virology Journal
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- 巻
- 11
- 号
- 1
- 開始ページ
- 122
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1186/1743-422X-11-122
- 出版者・発行元
- BioMed Central Ltd.
Background: HIV-1 Vif is essential for virus replication in natural target cells such as T cells and macrophages. Vif recruits a ubiquitin ligase to degrade restrictive APOBEC3 proteins. APOBEC3G is one of the most potent retroviral restriction factors targeted by Vif and, as such, the Vif-APOBEC3G interaction has emerged as a promising HIV-1 therapeutic target. Methods. 20,000 small molecules were used in live-cell screens for those that preserve EGFP-APOBEC3G fluorescence and luciferase-APOBEC3G luminescence in the presence of HIV-1 Vif. Results: 2 compounds with similar core structures preserved APOBEC3G levels in the presence of Vif. 10 μM of compound restored APOBEC3G to levels sufficient for incorporation into vif-proficient virus particles and restriction of virus infectivity. Vif-dependent APOBEC3G polyubiquitination and general proteasomal activity were unaffected at the same concentration. Conclusions: The small molecules described here preserve APOBEC3G levels and activity in the presence of Vif. These molecules are starting points for further development as antiretrovirals. © 2014 Matsui et al.
licensee BioMed Central Ltd.
licensee BioMed Central Ltd.
- リンク情報
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- DOI
- https://doi.org/10.1186/1743-422X-11-122
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/24986077
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84904216014&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84904216014&origin=inward
- ID情報
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- DOI : 10.1186/1743-422X-11-122
- ISSN : 1743-422X
- eISSN : 1743-422X
- PubMed ID : 24986077
- SCOPUS ID : 84904216014