Letter | Published:

Reassembled HVJ (Sendai virus) envelopes containing non-toxic mutant proteins of diphtheria toxin show toxicity to mouse L cell

Naturevolume 266pages839840 (1977) | Download Citation



PREVIOUS studies from this laboratory have described the preparation, from HVJ virions solubilised with a non-ionic detergent, of a reassembled envelope fraction free of nucleocapsids. Such reconstituted envelopes still retain neuraminidase, haemagglutinating, cell fusion and haemolytic activities1–3. Since intact virions release their nucleoproteins into the cytoplasm after fusion with mammalian cells, it seemed possible that any given macromolecule contained within such a reassembled viral envelope might be introduced into susceptible mammalian cells by this means. We report here the successful application of this method to the introduction of CRM45, a non-toxic mutant protein related to diphtheria toxin4, into mouse L cells, a strain that is normally toxin resistant. Although CRM45 is a potent NAD : elongation factor 2-ADP ribosyl (NAD : EF2-ADPR) transferase5,6 and thus blocks protein synthesis in eukaryotic cell extracts, it is non-toxic for animal cells because it lacks a C-terminal sequence of amino acids necessary to bind to susceptible cell membranes and thus cannot reach the cell interior7. If a few molecules of CRM45 could be introduced into the living cell cytoplasm, they should block protein synthesis and kill the cells. This has now been accomplished by fusion of CRM45-containing reassembled HVJ envelopes with cultured mouse L cells.

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  1. 1

    Hosaka, Y. & Shimizu, Y. K. Virology 49, 627–639 (1972).

  2. 2

    Shimizu, K., Hosaka, Y. & Shimizu, Y. K. J. Virol. 9, 842–850 (1972).

  3. 3

    Okada, Y., Hosaka, Y., Shimizu, K. & Matsui, K. Cell Struct. Funct. 1, 129–132 (1975).

  4. 4

    Uchida, T., Gill, D. M. & Pappenheimer, A. M., Jr Nature new Biol. 233, 8–11 (1971).

  5. 5

    Honjo, T., Nishizuka, Y., Kato, I. & Hayaishi, O. J. biol. Chem. 243, 3553–3555 (1968).

  6. 6

    Gill, D. M., Pappenheimer, A. M., Jr, Brown, R. & Kurnick, J. T. J. exp. Med. 129, 1–21 (1969).

  7. 7

    Uchida, T., Pappenheimer, A. M., Jr. & Harper, A. A. Science 175, 901–903 (1972).

  8. 8

    Gill, D. M. & Pappenheimer, A. M., Jr. J. biol. Chem. 246, 1492–1495 (1971).

  9. 9

    Drazin, R., Kandel, J. & Collier, R. J. J. biol. Chem. 246, 1504–1510 (1971).

  10. 10

    Magee, W. E. Nature 235, 339–341 (1972).

  11. 11

    Papahadjopoulos, D., Poste, D. & Maghew, E. Biochem. biophys. Acta 363, 401–418 (1974).

  12. 12

    Batzri, S. & Korn, E. D. J. cell. Biol. 66, 621–634 (1975).

  13. 13

    Furusawa, M., Nishimura, T., Yamaizumi, M. & Okaka, Y. Nature 249, 449–450 (1974).

  14. 14

    Loyter, A., Zakai, N. & Kulka, R. G. J. Cell Biol. 66, 292–304 (1975).

  15. 15

    Okada, Y. & Murayama, F. Expl Cell Res. 44, 527–551 (1966).

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  1. Research Institute for Microbial Diseases, Osaka University, Yamada-kami, Suita-City, Osaka, Japan



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