C - Chemistry – Metallurgy – 12 – N
Patent
C - Chemistry, Metallurgy
12
N
C12N 15/49 (2006.01) C07K 14/155 (2006.01) C07K 16/10 (2006.01) C12Q 1/68 (2006.01) G01N 33/569 (2006.01)
Patent
CA 2446460
The regulatory proteins Tat and Rev are essential to bovine immunodeficiency virus (BIV) replication at the transcriptional and post-transcriptional level, respectively. Previous studies have shown that BIV may encode two types of Tat proteins of 103 and 108 amino acids, respectively. Here, we report the identification and characterization of a new BIV Tat protein (composed of 236 amino acids) (Tat236) derived from a tat/rev cDNA. The tat/rev cDNA was obtained by reverse transcription-PCR from RNA extracted from cells infected with BIV isolated by co-cultivation of FBLU cells with the spleen cells of rabbits exposed for 3 years to the R29 isolate of BIV. Sequence analysis indicated that BIV Tat236 contains the first 98 amino acids of Tat103 and the 3' end 138 amino acids of Rev. Reporter gene assays indicated that transactivation of BIV long terminal repeat (LTR) by Tat236 is higher than by the original BIV Tat proteins in Cf2Th, FBLU, 293A and Hela cells. In addition, BIV Tat236 protein cross-transactivated the human immunodeficiency virus (HIV-1) promoter more efficiently than that observed with BIV Tat103 in Cf2Th cells. Tat236 deletion mutants showed that the predicted basic domain of Rev within Tat236 plays a major role in the observed enhanced transactivation activity of the protein. However, the intact functional domain of the original BIV Tat is required for efficient transactivation. This is the first report of a hybrid Tat protein from BIV or any lentiviruses that shows higher transactivation than the original transactivator Tat proteins.
Abed Yacine
Archambault Denis
St-Louis Marie-Claude
Abed Yacine
Archambault Denis
St-Louis Marie-Claude
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