D‐Penicillamine inhibits transactivation of human immunodeficiency virus type‐1 (HIV‐1) LTR by transactivator protein

FEBS Letters

Chandra, P.¹  Chandra, A.¹  Arya, S.K.²  Demirhan, I.¹ 

[1] Abteilung für Molekularbiologie (ZBC), Klinikum der Universität Frankfurt, Theodor-Stern-Kai 7, D-6 Frankfurt 70, FRG;Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20205, USA

关键词: D-Penicillamine;    HIV-1;    Transactivation;    tat protein: Azidothymidine;    AIDS;   

DOI  :  10.1016/0014-5793(88)80038-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

D-Penicillamine, an amino acid analogue of cysteine, has been shown to inhibit the transactivation of HIV-1 LTR by the transactivator protein, tat protein. The transactivation was studied in Jurkat cells co-transfected with plasmids containing HIV-LTR sequences fused to the bacterial chloramphenicol acetyltransferase (CAT) gene and HIV tat gene. The expression of CAT activity was a measure of transactivation of LTR by the tat protein. Incubation of transfected Jurkat cells with D-penicillamine led to inhibition of CAT activity. This inhibition was found to be concentration-dependent; more than 90% inhibition of chloramphenicol acetylation was seen in extracts prepared from cultures incubated with 40 μg/ml of D-penicillamine. Earlier experiments have shown that D-penicillamine at 40 μg/ml can completely inhibit HIV-1 (HTLV-III B) replication in H9 cells [(1986) Drug Res. 36, 184–186]. These results suggest that inhibition of transactivation may be the molecular mechanism involved in the inhibition of HIV-1 replication by D-penicillamine.

【 授权许可】

Unknown