Nature 287, 68 - 70 (04 September 1980); doi:10.1038/287068a0

An interferon-induced cellular enzyme is incorporated into virions

David Wallach & Michel Revel

Department of Virology, The Weizmann Institute of Science, Rehovot, Israel

The mechanisms by which interferon inhibits viral growth are only partially understood. Several enzymatic activities increase in cells shortly after treatment with interf eron¹⁻⁸. One of these enzymes, oligo-isoadenylate synthetase, synthesizes (2'−5') isoadenylate oligomers which strongly stimulate the activity of a cellular ribonuclease, RNaseF (ref. 7). Interferon also significantly increases the activity of a protein kinase which phosphorylates the initiation factor eIF-2 and can inhibit in vitro protein synthesis. Such interferon-induced enzymes, which affect RNA and protein metabolism, might be responsible for many of its effects on viruses. Indeed, inhibition of viral protein and RNA synthesis appears to have a major role in the antiviral state⁹. We have now investigated possible interactions of the two enzymes with viral constituents during the course of infection and found that in two different membrane-coated RNA viruses, vesicular stomatitis virus (VSV) and Moloney murine leukaemia virus (M-MuLV), there is an accumulation of the (2'−5') oligo-isoadenylate synthetase (E) in the virions. Most of the enzyme is bound to the virion ribonucleoprotein core. The incorporation of E into the virions suggests a direct involvement of the enzyme in regulation of virus functions.

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