scholarly journals Tat basic domain: A “Swiss army knife” of HIV-1 Tat?

2019 ◽  
Vol 29 (2) ◽  
pp. e2031 ◽  
Author(s):  
Margarita A. Kurnaeva ◽  
Eugene V. Sheval ◽  
Yana R. Musinova ◽  
Yegor S. Vassetzky
Keyword(s):  
Basic Domain ◽  
Hiv 1

scholarly journals Transduction of Cu,Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells

FEBS Letters ◽  
2000 ◽  
Vol 485 (2-3) ◽  
pp. 163-167 ◽  
Author(s):  
Hyeok Yil Kwon ◽  
Won Sik Eum ◽  
Hyun Woo Jang ◽  
Jung Hoon Kang ◽  
Jiyoon Ryu ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Mammalian Cells ◽  
Tat Protein ◽  
Basic Domain ◽  
Hiv 1

scholarly journals Role of the Gag Matrix Domain in Targeting Human Immunodeficiency Virus Type 1 Assembly

2000 ◽  
Vol 74 (6) ◽  
pp. 2855-2866 ◽  
Author(s):  
Akira Ono ◽  
Jan M. Orenstein ◽  
Eric O. Freed
Keyword(s):  
Human Immunodeficiency Virus ◽  
Plasma Membrane ◽  
Virus Particle ◽  
Particle Formation ◽  
Membrane Targeting ◽  
Basic Domain ◽  
Golgi Vesicles ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) particle formation and the subsequent initiation of protease-mediated maturation occur predominantly on the plasma membrane. However, the mechanism by which HIV-1 assembly is targeted specifically to the plasma membrane versus intracellular membranes is largely unknown. Previously, we observed that mutations between residues 84 and 88 of the matrix (MA) domain of HIV-1 Gag cause a retargeting of virus particle formation to an intracellular site. In this study, we demonstrate that the mutant virus assembly occurs in the Golgi or in post-Golgi vesicles. These particles undergo core condensation in a protease-dependent manner, indicating that virus maturation can occur not only on the plasma membrane but also in the Golgi or post-Golgi vesicles. The intracellular assembly of mutant particles is dependent on Gag myristylation but is not influenced by p6Gag or envelope glycoprotein expression. Previous characterization of viral revertants suggested a functional relationship between the highly basic domain of MA (amino acids 17 to 31) and residues 84 to 88. We now demonstrate that mutations in the highly basic domain also retarget virus particle formation to the Golgi or post-Golgi vesicles. Although the basic domain has been implicated in Gag membrane binding, no correlation was observed between the impact of mutations on membrane binding and Gag targeting, indicating that these two functions of MA are genetically separable. Plasma membrane targeting of Gag proteins with mutations in either the basic domain or between residues 84 and 88 was rescued by coexpression with wild-type Gag; however, the two groups of MA mutants could not rescue each other. We propose that the highly basic domain of MA contains a major determinant of HIV-1 Gag plasma membrane targeting and that mutations between residues 84 and 88 disrupt plasma membrane targeting through an effect on the basic domain.

Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells

2001 ◽  
Vol 31 (11) ◽  
pp. 1509-1519 ◽  
Author(s):  
Li Hua Jin ◽  
Jae Hoon Bahn ◽  
Won Sik Eum ◽  
Hyeok Yil Kwon ◽  
Sang Ho Jang ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Tat Protein ◽  
Basic Domain ◽  
Hiv 1

scholarly journals A Naturally Occurring Polymorphism in the HIV-1 Tat Basic Domain Inhibits Uptake by Bystander Cells and Leads to Reduced Neuroinflammation

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Arthur P. Ruiz ◽  
David O. Ajasin ◽  
Santhamani Ramasamy ◽  
Vera DesMarais ◽  
Eliseo A. Eugenin ◽  
...  
Keyword(s):  
Basic Domain ◽  
Naturally Occurring ◽  
Bystander Cells ◽  
Hiv 1

scholarly journals BSA conjugates bearing multiple copies of the basic domain of HIV-1 Tat: Prototype for the development of multitarget inhibitors of extracellular Tat

2010 ◽  
Vol 87 (1) ◽  
pp. 30-39 ◽  
Author(s):  
Antonella Bugatti ◽  
Paola Chiodelli ◽  
Joseph Rosenbluh ◽  
Abraham Loyter ◽  
Marco Rusnati
Keyword(s):  
Basic Domain ◽  
Multiple Copies ◽  
Hiv 1

scholarly journals Complexes of Plasmid DNA with Basic Domain 47-57 of the HIV-1 Tat Protein Are Transferred to Mammalian Cells by Endocytosis-mediated Pathways

2003 ◽  
Vol 278 (43) ◽  
pp. 42625-42636 ◽  
Author(s):  
Irina A. Ignatovich ◽  
Ella B. Dizhe ◽  
Anna V. Pavlotskaya ◽  
Boris N. Akifiev ◽  
Sergey V. Burov ◽  
...  
Keyword(s):  
Plasmid Dna ◽  
Mammalian Cells ◽  
Tat Protein ◽  
Basic Domain ◽  
Hiv 1
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