Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif

Journal of Virology
F FengPeng Li

Abstract

Virion infectivity factor (Vif) protein of human immunodeficiency virus type 1 (HIV-1) is essential for the productive infection of primary human CD4 T lymphocytes and macrophages. Vif overcomes the HIV-inhibitory effects of cellular factor APOBEC3G, which has cytidine deaminase activity. We previously reported the isolation of a Vif-interacting ring finger protein, Triad 3, from a human leukocyte cDNA library, using the yeast two-hybrid system. The full-length cellular protein homologue of Triad 3 has been recently identified as the zinc finger protein inhibiting NF-kappaB (ZIN). Sequence analysis indicates that Triad 3 protein contains all four major ring-like motifs of ZIN. We report here that ZIN binds to purified Vif in vitro and that Triad 3/ZIN interacts with HIV-1 Vif in transfected human 293T cells, as demonstrated by coimmunoprecipitation. To test the biological relevance of this interaction, we produced infectious HIV-1 NL4.3 in the presence or absence of cotransfected ZIN. HIV-1 NL4.3 virus stocks produced in the presence of exogenously expressed ZIN were twofold less infectious in a single-cycle infectivity assay than virus produced in the absence of exogenous ZIN. It was further shown that cells infected with HIV ...Continue Reading

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Citations

Sep 3, 2010·Amino Acids·Daniela GalleranoRudolf Valenta
Mar 21, 2007·Genome Biology·Birgit EisenhaberMarie-Theres Hauser
Dec 23, 2015·Respirology : Official Journal of the Asian Pacific Society of Respirology·Feng FengPaul N Reynolds
Mar 1, 2014·The Biochemical Journal·Donald E SprattGary S Shaw

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