This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Feng, F. Articles by Li, P. Search for Related Content PubMed PubMed Citation Articles by Feng, F. Articles by Li, P.

 Previous Article  |  Next Article 

Journal of Virology, October 2004, p. 10574-10581, Vol. 78, No. 19
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.19.10574-10581.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Ring Finger Protein ZIN Interacts with Human Immunodeficiency Virus Type 1 Vif

Australian Centre for Hepatitis and HIV Virology Research, Infectious Diseases Laboratories, Institute of Medical and Veterinary Science,¹ School of Molecular Biosciences, University of Adelaide, Adelaide, Australia²

Received 4 December 2003/ Accepted 21 May 2004

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-B (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 NL4.3 virus stocks produced in the presence of exogenously expressed ZIN were impaired in viral DNA synthesis by twofold. The impairment in viral reverse transcription and the reduction in single-cycle viral infectivity were both shown to be dependent on the presence of Vif in the virus producer cells. The possible mechanisms by which ZIN interferes with the early events of HIV-1 replication are discussed.

This article has been cited by other articles:

• Burnett, A., Spearman, P. (2007). APOBEC3G Multimers Are Recruited to the Plasma Membrane for Packaging into Human Immunodeficiency Virus Type 1 Virus-Like Particles in an RNA-Dependent Process Requiring the NC Basic Linker. J. Virol. 81: 5000-5013 [Abstract] [Full Text]  
• Liu, B., Sarkis, P. T. N., Luo, K., Yu, Y., Yu, X.-F. (2005). Regulation of Apobec3F and Human Immunodeficiency Virus Type 1 Vif by Vif-Cul5-ElonB/C E3 Ubiquitin Ligase. J. Virol. 79: 9579-9587 [Abstract] [Full Text]  
• Wichroski, M. J., Ichiyama, K., Rana, T. M. (2005). Analysis of HIV-1 Viral Infectivity Factor-mediated Proteasome-dependent Depletion of APOBEC3G: CORRELATING FUNCTION AND SUBCELLULAR LOCALIZATION. J. Biol. Chem. 280: 8387-8396 [Abstract] [Full Text]