ArticleMolecular and cellular biochemistry2010
Effect of the redox state on HIV-1 tat protein multimerization and cell internalization and trafficking.
Article in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- HIV-1 Tat and Heparan Sulfate Proteoglycans Orchestrate the Setup ofMolecules (Basel, Switzerland) · 2021Article
- HIV-1 Tat Protein Enters Dysfunctional Endothelial Cells via Integrins and Renders Them Permissive to Virus Replication.International journal of molecular sciences · 2020Article
- Review
- Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019Review
- HEXIM1-Tat chimera inhibits HIV-1 replication.PLoS pathogens · 2018Article
- HIV Tat protein and amyloid-β peptide form multifibrillar structures that cause neurotoxicity.Nature structural & molecular biology · 2017Article
- Didehydro-cortistatin A inhibits HIV-1 Tat mediated neuroinflammation and prevents potentiation of cocaine reward in Tat transgenic mice.Current HIV research · 2015Article
- HIV-1, reactive oxygen species, and vascular complications.Free radical biology & medicine · 2012Review
- The HIV-1 transactivator factor (Tat) induces enterocyte apoptosis through a redox-mediated mechanism.PloS one · 2011Article
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The redox state of the cysteine-rich region of the HIV Tat protein is known to play a crucial role in Tat biological activity. In this article, we show that Tat displays two alternative functional states depending on the presence of either one or three reduced sulphydryl groups in the cysteine-rich region, respectively. Using different approaches, a disulfide pattern has been defined for the Tat protein and a specific DTT-dependent breaking order of disulfide bonds highlighted. The Tat redox state deeply influences macrophage protein uptake. Immunoistochemistry analysis shows that the oxidized protein does not enter cells, whereas partially reduced protein reaches the cytosol and, to a limited extent, the nucleus. Finally electrophoretic analysis shows Tat high-molecular weight multi-aggregation, resulting in the loss of biological activity. This is due to strong electrostatic and metal-binding interactions, whereas Tat dimerization involves metal-binding interactions as well as disulfide bond formation.
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