Letter | Published:

An interferon-induced cellular enzyme is incorporated into virions

Naturevolume 287pages6870 (1980) | Download Citation

Subjects

Abstract

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.

References

  1. 1

    Roberts, W. K., Hovanessian, A., Brown, R. E., Clemens, M. J. & Kerr, I. M. Nature 264, 477–480 (1976).

  2. 2

    Revel, M. et al. in Proc. 11th FEBS Meet. 43, 47–58 (1977).

  3. 3

    Kerr, I. M. & Brown, R. E. Proc. natn. Acad. Sci. U.S.A. 75, 256–260 (1978).

  4. 4

    Zilberetein, A., Kimchi, A., Schmidt, A. & Revel, M. Proc. natn. Acad. Sci. U.S.A. 75, 4734–4738 (1978).

  5. 5

    Farrell, P. J. et al. Proc. natn. Acad. Sci. U.S.A. 75, 5893–5897 (1978).

  6. 6

    Kimchi, A. et al. Proc. natn. Acad. Sci. U.S.A. 76, 3208–3212 (1979).

  7. 7

    Schmidt, A. et al. FEBS Lett. 95, 257–264 (1978).

  8. 8

    Cooper, J. A. & Farrell, P. J. Biochem. biophys. Res. Commun. 77, 124–131 (1977).

  9. 9

    Friedman, R. M. & Chang, E. H. in Interferons and their Actions (ed. Stewart, W. E. II) 145–152 (CRC Press, Ohio, 1977).

  10. 10

    Hovanessian, A. G., Brown, R. E. & Kerr, I. M. Nature 268, 537–539 (1977).

  11. 11

    Nilsen, T. W. & Baglioni, C. Proc. natn. Acad. Sci. U.S.A. 76, 2600–2604 (1979).

  12. 12

    Galster, R. L. & Lengyl, P. Nucleic Acids Res. 3, 581–598 (1976).

  13. 13

    Aujean, O., Sanceau, J., Falcoff, E. & Falcoff, R. Virology 92, 583–586 (1979).

  14. 14

    Pitha, P. M., Rowe, W. P. & Oxman, M. N. Virology 70, 324–338 (1976).

  15. 15

    Wong, P. K. Y. et al. Cell 10, 245–252 (1977).

  16. 16

    Chang, E. H. & Friedman, R. M. Biochem. biophys. Res. Commun. 77, 392–398 (1977).

  17. 17

    Bandyopadhyay, A. K., Chang, E. H., Levy, C. C. & Friedman, R. M. Biochem. biophys. Res. Commun. 87, 983–988 (1979).

  18. 18

    Salzberg, S., Bakhanashvili, M. & Aboud, M. J. gen. Virol. 40, 121–130 (1978).

Download references

Author information

Affiliations

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

    • David Wallach
    •  & Michel Revel

Authors

  1. Search for David Wallach in:

  2. Search for Michel Revel in:

About this article

Publication history

Received

Accepted

Issue Date

DOI

https://doi.org/10.1038/287068a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.