Inhibition of the synthesis of Moloney leukemia virus structural proteins by N-methylisatin-beta-4',4'-diethylthiosemicarbazone
Author(s) -
D Ronen,
Yael Teitz
Publication year - 1984
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.26.6.913
Subject(s) - murine leukemia virus , protein biosynthesis , intracellular , virus , leukemia , rna , biology , microbiology and biotechnology , beta (programming language) , structural protein , leucine , reverse transcriptase , virology , chemistry , biochemistry , amino acid , immunology , gene , computer science , programming language
The mechanism of inhibition of Moloney leukemia virus by N-methylisatin-beta-4',4'-diethylthiosemicarbazone was studied. Experiments that used [3H]leucine for short-pulse labeling in the presence of the drug resulted in a 71% inhibition in the synthesis of Pr-80, the polypeptide precursor of the gag viral proteins. The radioactive pulse products of the polypeptide precursors after a further 2-h chase period showed a normal cleavage of the precursors, with the formation of a reduced amount of final mature viral structural proteins. The experimental evidence indicated that at the inhibitory concentration of 17 microM N-methylisatin-beta-4',4'-diethylthiosemicarbazone, the amount of intracellular viral RNA was not affected, whereas the activities of reverse transcriptase and the other viral protein syntheses were suppressed.
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