Location of the
            <i>Trans</i>
            -Activating Region on the Genome of Human T-Cell Lymphotropic Virus Type III

Sodroski, Joseph; Patarca, Roberto; Rosen, Craig A.; Wong‐Staal, Flossie; Haseltine, William A.

doi:10.1126/science.2990041

Cited by 541 publications

(283 citation statements)

References 36 publications

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“…Our data also show that the pBENN-2 plasmid, which encodes the HIV tat, likewise appears to trans-activate primarily at the level of increased mRNA. This finding is in agreement with a report by Peterlin et al (14) but conflicts with another report (7) showing that HIV tat produces more stimulation at the protein level than is seen at the level of mRNA. We find that the HIV DNA sequences required for stimulation by tat are not required for stimulation by the HCMV TE region.…”

Section: Discussionsupporting

confidence: 91%

Immediate-early gene region of human cytomegalovirus trans-activates the promoter of human immunodeficiency virus.

Davis

Kenney²,

Kamine³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

292

142

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Section: Discussionsupporting

confidence: 91%

Immediate-early gene region of human cytomegalovirus trans-activates the promoter of human immunodeficiency virus.

Davis

Kenney²,

Kamine³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

292

142

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“…Tat is essential for viral replication, transmission and disease progression [1,[4][5][6][7]. In addition, Tat can modulate the expression of cytokines and cellular genes [6][7][8][9][10][11], and chemokine receptors [12][13][14][15], which are responsible for the transmission of macrophageand T-cell-tropic HIV-1 strains, respectively.…”

Section: Introductionmentioning

confidence: 99%

Long-term protection against SHIV89.6P replication in HIV-1 Tat vaccinated cynomolgus monkeys

Maggiorella

Baroncelli

Michelini

et al. 2004

Vaccine

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Vaccination with a biologically active Tat protein or tat DNA contained infection with the highly pathogenic SHIV89.6P virus, preventing CD4 T-cell decline and disease onset. Here we show that protection was prolonged, since neither CD4 T-cell decline nor active virus replication was observed in all vaccinated animals that controlled virus replication up to week 104 after the challenge. In contrast, virus persisted and replicated in peripheral blood mononuclear cells and lymph nodes of infected animals, two of which died. Tat-specific antibody, CD4 and CD8 T-cell responses were high and stable only in the animals controlling the infection. In contrast, Gag-specific antibody production and CD4 and CD8 T-cell responses were consistently and persistently positive only in the monkeys that did not control primary virus replication. These results indicate that vaccination with Tat protein or DNA induced long-term memory Tat-specific immune responses and controlled primary infection at its early stages allowing a long-term containment of virus replication and spread in blood and tissues.

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“…HIV-1 tat is an 86-amino acid-long protein, which greatly increases viral gene expression and replication (2,4,13,14,34,35). The tripeptide RGD sequence in tat is 10-Dr.…”

mentioning

confidence: 99%

Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human immunodeficiency virus type 1 transactivation protein, tat.

Brake

Debouck

Biesecker

1990

The Journal of Cell Biology

172

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Abstract. Tat, the transactivation factor of human immunodeflciency virus type 1 (HIV-1), contains the highly conserved tripeptide sequence Arg-Gly-Asp (RGD) that characterizes sites for integrin-mediated cell adhesion. The tat protein was assayed for cell attachment activity by measuring the adhesion of monocytic, T lymphocytic, and skeletal muscle-derived cell lines to tat-coated substratum. All cell lines tested bound to tat in a dose-dependent manner and the tat cell adhesion required the RGD sequence because tat mutants constructed to contain an RGE or KGE tripeptide sequence did not mediate efficient cell adhesion. The tat-mediated cell attachment also required divalent cations and an intact cytoskeleton. In addition, cell adhesion to tat was inhibited in the presence of an RGD-containing peptide GRGDSPK or an antitat mAb that recognizes the RGD epitope. These results strongly suggest that cells are bound to tat through an integrin. Interestingly, myoblast cells bound to tat remained round, whereas the same cells attached through an integrin for a matrix protein typicaUy flatten and spread. The role of this RGD-dependent cellular adhesion of tat in HIV-1 infection remains to be determined.p ROTEINS that interact with integrin cell adhesion receptors frequently contain the amino acid tripeptide RGD sequence (5,20,26,30) within the integrin binding site. RGD sequences are found in fibronectin, vitronectin and collagen and constitute extracellular matrix attachment sites used for integrin-mediated cell adherence during development and differentiation (30). Integrin receptors on leukocytes bind to coagulation proteins (von Willebrand factor, fibrinogen, thrombospondin) and complement components (C3b), and participate in cell-cell adhesion (LFA-1 with I-CAM). These interactions are involved in homeostatic regulation, phagocytosis, cell migration, cell signaling, cellular trafficking, and lymphocyte recognition (11, 23,30,39). In addition, certain bacterial, parasitic, and viral proteins possess RGD sequences which recognize integrin receptors and may contribute to pathogenesis (1, 30, 31).Human immunodeficiency virus type I (HIV-1),~ the etiologic agent of AIDS (6,17,22,28), encodes a gene for a transactivating protein, termed tat, which contains an RGD sequence. HIV-1 tat is an 86-amino acid-long protein, which greatly increases viral gene expression and replication (2,4,13,14,34,35). The tripeptide RGD sequence in tat is 10-Dr. Brake's present address is Biological Research, SmithKline Beecham Animal Health Products, King of Prussia, PA, 19406-0939. Address all correspondence to Dr. C: Debouck. cated in the carboxy-terminal portion of the protein and is highly conserved among HW-1 isolates (Fig. 1) (24). The presence of an RGD sequence within tat raised the intriguing possibility that this tripeptide could constitute a cell attachment site. In this study, purified tat protein was assayed for cell attachment to various cell types. The observed cell adhesion was further characterized using an RGD-containing pep...

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Location of the Trans -Activating Region on the Genome of Human T-Cell Lymphotropic Virus Type III

Cited by 541 publications

References 36 publications

Immediate-early gene region of human cytomegalovirus trans-activates the promoter of human immunodeficiency virus.

Immediate-early gene region of human cytomegalovirus trans-activates the promoter of human immunodeficiency virus.

Long-term protection against SHIV89.6P replication in HIV-1 Tat vaccinated cynomolgus monkeys

Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human immunodeficiency virus type 1 transactivation protein, tat.

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