| Literature DB >> 27007880 |
Xuechao Zhao1, Lingyu Qian1, Deyu Zhou1, Di Qi1, Chang Liu1, Xiaohong Kong2.
Abstract
The multifunctional trans-activator Tat is an essential regulatory protein for HIV-1 replication and is characterized by high sequence diversity. Numerous experimental studies have examined Tat in HIV-1 subtype B, but research on subtype C Tat is lacking, despite the high prevalence of infections caused by subtype C worldwide. We hypothesized that amino acid differences contribute to functional differences among Tat proteins. In the present study, we found that subtype B NL4-3 Tat and subtype C isolate HIV1084i Tat exhibited differences in stability by overexpressing the fusion protein Tat-Flag. In addition, 1084i Tat can activate LTR and NF-κB more efficiently than NL4-3 Tat. In analyses of the activities of the truncated forms of Tat, we found that the carboxyl-terminal region of Tat regulates its stability and transactivity. According to our results, we speculated that the differences in stability between B-Tat and C-Tat result in differences in transactivation ability.Entities:
Keywords: NF-κB activation; Tat; carboxyl-terminal region; stability; subtype B/C; transactivation
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Year: 2016 PMID： 27007880 PMCID： PMC8193441 DOI： 10.1007/s12250-016-3681-0
Source DB: PubMed Journal: Virol Sin ISSN： 1995-820X Impact factor: 4.327