Abstract:
:The human immunodeficiency virus type 1 (HIV-1) Tat protein is essential for viral replication and stimulates transcription of the integrated provirus by recruiting the kinase complex TAK/P-TEFb, composed of cyclin T1 (CycT1) and Cdk9, to the viral TAR RNA element. TAK/P-TEFb phosphorylates the RNA polymerase II complex and stimulates transcriptional elongation. In this report, we investigated the regulation of TAK/P-TEFb in primary human macrophages, a major target cell of HIV infection. While Cdk9 levels remained constant, CycT1 protein expression in freshly isolated monocytes was very low, increased early during macrophage differentiation, and, unexpectedly, decreased to very low levels after about 1 week in culture. The kinase activity of TAK/P-TEFb paralleled the changes in CycT1 protein expression. RNA analysis indicated that the transient induction of CycT1 protein expression involves a posttranscriptional mechanism. In transient transfection assays, the ability of Tat to transactivate the HIV long terminal repeat (LTR) in the late differentiated macrophages was greatly diminished relative to its ability to transactivate the HIV LTR in early differentiated cells, strongly suggesting that CycT1 is limiting for Tat function in late differentiated macrophages. Interestingly, lipopolysaccharide, a component of the cell wall of gram-negative bacteria, reinduced CycT1 expression late in macrophage differentiation. These results raise the possibility that regulation of CycT1 expression may be involved in establishing latent infection in macrophages and that opportunistic infection may reactivate the virus by inducing CycT1 expression.
journal_name
J Viroljournal_title
Journal of virologyauthors
Liou LY,Herrmann CH,Rice APdoi
10.1128/jvi.76.21.10579-10587.2002subject
Has Abstractpub_date
2002-11-01 00:00:00pages
10579-87issue
21eissn
0022-538Xissn
1098-5514journal_volume
76pub_type
杂志文章abstract::This paper describes Q beta noninfectious particles produced at 41 degrees C in a streptomycin-resistant Escherichia coli mutant which is temperature sensitive for suppression of a nonsense codon. The noninfectious particles resembled Q beta under the electron microscope and contained coat protein molecules in an amou...
journal_title:Journal of virology
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doi:10.1128/JVI.29.3.1107-1117.1979
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pub_type: 杂志文章
doi:10.1128/JVI.40.3.691-702.1981
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journal_title:Journal of virology
pub_type: 杂志文章
doi:10.1128/JVI.40.3.752-761.1981
更新日期:1981-12-01 00:00:00
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journal_title:Journal of virology
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pub_type: 杂志文章
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journal_title:Journal of virology
pub_type: 杂志文章
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pub_type: 杂志文章
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