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Tat is a Multifunctional Viral Protein That Modulates Cellular Gene Expression and Functions

Overview
Journal Oncotarget
Specialty Oncology
Date 2017 Feb 11
PMID 28187438
Citations 57
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Abstract

The human immunodeficiency virus type I (HIV-1) has developed several strategies to condition the host environment to promote viral replication and spread. Viral proteins have evolved to perform multiple functions, aiding in the replication of the viral genome and modulating the cellular response to the infection. Tat is a small, versatile, viral protein that controls transcription of the HIV genome, regulates cellular gene expression and generates a permissive environment for viral replication by altering the immune response and facilitating viral spread to multiple tissues. Studies carried out utilizing biochemical, cellular, and genomic approaches show that the expression and activity of hundreds of genes and multiple molecular networks are modulated by Tat via multiple mechanisms.

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References
1.
Tahirov T, Babayeva N, Varzavand K, Cooper J, Sedore S, Price D . Crystal structure of HIV-1 Tat complexed with human P-TEFb. Nature. 2010; 465(7299):747-51. PMC: 2885016. DOI: 10.1038/nature09131. View

2.
Mocchetti I, Bachis A, Avdoshina V . Neurotoxicity of human immunodeficiency virus-1: viral proteins and axonal transport. Neurotox Res. 2011; 21(1):79-89. PMC: 4089041. DOI: 10.1007/s12640-011-9279-2. View

3.
Verhoef K, Bauer M, Meyerhans A, Berkhout B . On the role of the second coding exon of the HIV-1 Tat protein in virus replication and MHC class I downregulation. AIDS Res Hum Retroviruses. 1998; 14(17):1553-9. DOI: 10.1089/aid.1998.14.1553. View

4.
Benelli R, Barbero A, Ferrini S, Scapini P, Cassatella M, Bussolino F . Human immunodeficiency virus transactivator protein (Tat) stimulates chemotaxis, calcium mobilization, and activation of human polymorphonuclear leukocytes: implications for Tat-mediated pathogenesis. J Infect Dis. 2000; 182(6):1643-51. DOI: 10.1086/317597. View

5.
Bayer P, Kraft M, Ejchart A, Westendorp M, Frank R, Rosch P . Structural studies of HIV-1 Tat protein. J Mol Biol. 1995; 247(4):529-35. DOI: 10.1006/jmbi.1995.0158. View