The production of Moloney murine leukaemia virus from chronically infected cells was inhibited after starvation of glutamine. While the rate of synthesis of the precursor of the core proteins, Pr65, was not affected in the starved cells, its proteolytic processing was blocked. Pulse-chase experiments indicated that glutamine was required during the synthesis of Pr65 to facilitate its subsequent processing. In addition, the synthesis of Pr200, the precursor of the protease, reverse transcriptase and endonuclease, was inhibited in the glutamine-starved cells. Starvation for other essential amino acids such as tyrosine and isoleucine affected neither the synthesis nor the processing of the virus proteins. These results suggest that the readthrough mechanism which enables synthesis of the Pr200 polyprotein is modulated in the chronically infected cells by glutamine levels. Since the viral protease is part of the gene, its synthesis may be inhibited in the glutamine-starved cells and Pr65 is therefore not processed.


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