scholarly journals Inhibition of Human T Cell Leukaemia Virus Type I Long Terminal Repeat Expression by DNA Methylation: Implications for Latency

1994 ◽  
Vol 75 (11) ◽  
pp. 3255-3259 ◽  
Author(s):  
S. Cassens ◽  
U. Ulrich ◽  
P. Beimling ◽  
D. Simon
Keyword(s):  
Dna Methylation ◽  
T Cell ◽  
Long Terminal Repeat ◽  
Virus Type ◽  
Terminal Repeat ◽  
Cell Leukaemia ◽  
Type I ◽  
Leukaemia Virus ◽  
Human T Cell

scholarly journals The rapamycin sensitivity of human T-cell leukaemia virus type I-induced T-cell proliferation is mediated independently of the polypyrimidine motifs in the 5′ long terminal repeat

2001 ◽  
Vol 82 (2) ◽  
pp. 435-439 ◽  
Author(s):  
Nicola J. Rose ◽  
Andrew M. L. Lever
Keyword(s):  
T Cell ◽  
Long Terminal Repeat ◽  
Virus Type ◽  
Terminal Repeat ◽  
Cell Leukaemia ◽  
Type I ◽  
Messenger Rnas ◽  
Leukaemia Virus ◽  
Human T Cell

The immunosuppressant rapamycin can regulate the translation of a subset of messenger RNAs, a phenotype which has been linked to the presence of a polypyrimidine motif [C(N)4–14] downstream of the mRNA cap structure. T-cell clones naturally infected with transcriptionally active human T-cell leukaemia virus, type I (HTLV-I) undergo autologous proliferation; this phenotype is inhibited by rapamycin but not FK506, which reverses the rapamycin effect. Within the R region of the HTLV-I 5′ long terminal repeat (LTR) there are seven polypyrimidine motifs. We sought to determine if these were involved in the sensitivity of proliferation to the presence of rapamycin. Here we illustrate the generation of an in vitro model of this rapamycin-sensitivity and the analysis of LTR mutants which were created to determine the importance of the polypyrimidine motifs. Reporter gene assays suggest the effect is independent of the polypyrimidine motifs in the virus leader sequence.

Protective effect of interferon ? on human T cell leukaemia virus type I infection of CD4+ T cells isolated from human cord blood

1993 ◽  
Vol 37 (2) ◽  
pp. 97-104 ◽  
Author(s):  
Beatrice Macchi ◽  
Isabella Faraoni ◽  
Antonio Mastino ◽  
Chiara D'Onofrio ◽  
Gianna Romeo ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Protective Effect ◽  
Cord Blood ◽  
Virus Type ◽  
Cell Leukaemia ◽  
Type I ◽  
Human Cord Blood ◽  
Leukaemia Virus ◽  
Human T Cell

NEGATIVE ASSOCIATION BETWEEN THE HUMAN T-CELL LEUKAEMIA VIRUS TYPE I AND LARGE GRANULAR LYMPHOCYTE LEUKAEMIA IN JAPAN

The Lancet ◽  
1988 ◽  
Vol 332 (8617) ◽  
pp. 962 ◽  
Author(s):  
Nobutaka Imamura ◽  
Atsushi Kuramoto ◽  
Keisei Kawa-Ha ◽  
Hiroshi Fujii ◽  
Tomoo Takiguchi
Keyword(s):  
T Cell ◽  
Virus Type ◽  
Negative Association ◽  
Large Granular Lymphocyte ◽  
Cell Leukaemia ◽  
Type I ◽  
Leukaemia Virus ◽  
Human T Cell ◽  
Large Granular Lymphocyte Leukaemia

A 36-kilodalton cellular transcription factor mediates an indirect interaction of human T-cell leukemia/lymphoma virus type I TAX1 with a responsive element in the viral long terminal repeat

1990 ◽  
Vol 10 (8) ◽  
pp. 4192-4201
Author(s):  
S J Marriott ◽  
P F Lindholm ◽  
K M Brown ◽  
S D Gitlin ◽  
J F Duvall ◽  
...  
Keyword(s):  
T Cell ◽  
Long Terminal Repeat ◽  
Virus Type ◽  
Terminal Repeat ◽  
Type I ◽  
Indirect Interaction ◽  
T Cell Leukemia ◽  
Cell Leukemia ◽  
Human T Cell ◽  
Responsive Element

The human T-cell leukemia/lymphoma virus type I (HTLV-I) trans activator, TAX1, interacts indirectly with a TAX1-responsive element, TRE-2, located at positions -117 to -163 in the viral long terminal repeat. This report describes the characterization of a 36-kilodalton (kDa) protein identified in HeLa nuclear extract which mediates the interaction of TAX1 with TRE-2. Purification of the protein was achieved by zinc chelate chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The renatured 36-kDa protein bound specifically to a TRE-2 oligonucleotide but not to nonfunctional base substitution mutant probes in a gel retardation assay. Renatured proteins of differing molecular weights were unable to form this complex. In addition, the 36-kDa protein specifically activated transcription from the HTLV-I promoter in vitro. Purified TAX1 protein formed a complex with the TRE-2 oligonucleotide in the presence of the 36-kDa protein, suggesting that indirect interaction of TAX1 with the viral long terminal repeat may be one of the mechanisms by which HTLV-I transcription is regulated.

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