作者: Paul M. Loewenstein , Masaho Ishino , Na’eem Abdullah , Maurice Green
DOI: 10.1007/978-1-4684-5928-9_14
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摘要: The HIV-1 Tat protein is a potent transactivator that essential for virus replication. We reported previously chemically synthesized minimal domain peptides and full length (Tat86), in which alanine substituted Lys-41, are taken up by cells antagonize the expression of microinjected HIV-LTR driven CAT gene. find several mutant inhibit (HTLV-IIIB) Tat86,41Ala, most active peptide, inhibits replication 95–99% acutely infected when added to culture medium at concentrations 10−6 M 10−7 M; chronically also inhibited but lesser extent. Tat86,41Ala protects from virus-induced cytopathogenicity syncytia formation. mechanism inhibition unknown. Unexpectedly, co-transfection Tat86 expressing plasmid with plasmids does not transactivation endogenous HIV-LTRCAT HeLa cells. Thus together can block transactivation, expressed endogenously plasmid. These results imply novel antagonism.