Hostname: page-component-cc8bf7c57-n7pht Total loading time: 0 Render date: 2024-12-11T22:12:45.207Z Has data issue: false hasContentIssue false

Antigenic properties of the envelope of influenza virus rendered soluble by surfactant-solvent systems

Published online by Cambridge University Press:  15 May 2009

N. M. Larin
Affiliation:
Research Division, Pfizer Limited, Sandwich, Kent
P. H. Gallimore
Affiliation:
Research Division, Pfizer Limited, Sandwich, Kent
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Dissociating chemical treatments employing surfactant-solvent systems were applied to purified influenza A and B viruses to obtain viral preparations possessing a significantly higher or lower haemagglutinating activity than the intact virus. All preparations, whether with high or low haemagglutinating activity, with the exception of envelope protein solubilized by Triton X-100, were significantly lacking in the ability to excite the formation of haemagglutination-inhibiting and virus-neutralizing antibodies in inoculated ferrets. In contrast to other treatments, Triton X-100 treatment of virus significantly enhanced the antigenicity of viral protein as judged by virus neutralization and haemaggmtination inhibition tests. Yet the haemagglutinating activity of the envelope protein solubilized with Triton X-100 was about 1 % that of the intact virus. Results suggest that the correlation assumed to exist between the haemagglutinating activity of influenza virus and its ability to excite the formation of humoral antibodies is coincidental. Another important point is that the specific antigenicity of viral protein may be lost or enhanced owing to effects, other than solubilization, by surface-active agents.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1971

References

REFERENCES

Bonsall, R. W. & Hunt, S. (1966). Solubilization of a glucose binding component of the red cell membrane. Nature, London 211, 1368–70.CrossRefGoogle ScholarPubMed
Bradford, H. F., Swanson, P. D. & Gammack, D. B. (1964). Constituents of a microsomal fraction from the mammalian brain; their solubilization especially by detergents. Biochemical Journal 92, 247.CrossRefGoogle ScholarPubMed
Choppin, P. W. & Stoeckenius, W. (1964). Interactions of ether-disrupted influenza A2 virus with erythrocytes, inhibitors and antibodies. Virology 22, 482–92.CrossRefGoogle ScholarPubMed
Cleeland, R. & Sugg, J. Y. (1964). Serologic and antigenic properties of type A influenza virus after trypsin treatment. Journal of Immunology 93, 414–19.Google Scholar
Elworthy, P. H., Florence, A. T. & Macfarlane, C. B. (1968). Solubilization by Surface-Active Agents, pp. 11322. London: Chapman and Hall Ltd.Google Scholar
Fiset, P. (1964). Techniques in Experimental Virology, pp. 238–40. Ed. Harris, R. J. C.. London and New York: Academic Press.Google Scholar
Hobson, D., Lane, A., Beare, A. S. & Chivers, C. P. (1964). Serological studies on adult volunteers inoculated with oil-adjuvant Asian, influenza vaccine. British Medical Journal ii, 271–4.Google Scholar
Hobson, D. (1966). The strain specific serological activity of a non-haemagglutinating fraction of influenza viruses. British Journal of Experimental Pathology 47, 257–65.Google Scholar
Kandutsch, A. A. & Stimpfling, J. H. (1962). An isoantigenic lipoprotein from Sarcoma 1. CIBA Foundation Symposium, Transplantation, pp. 7289. Ed. Wostenholm, G. E. W. and Cameron, M. P..CrossRefGoogle Scholar
Larin, N. M. & Gallimore, P. H. (1971). The kinetics of influenza virus adsorption on iron oxide in the process of viral purification and concentration. Journal of Hygiene 69, 27.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurements with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–75.Google Scholar
Neurath, A. R., Rubin, B. A. & Pierzschala, W. A. (1967). Heterogeneity of V-antigens obtained by disruption of influenza viruses. Zeitschrift für Naturforschung 226, 850–5.Google Scholar
Neurath, A. R., Rubin, B. A. & Hartzell, R. W. (1969). Release of neuraminidase from haemagglutinins caused by treatment of influenza viruses with ether. Archiv für die gesamte Virusforschung 28, 421–3.Google Scholar
Pepper, D. C. (1967). A chromatographic procedure for the purification of influenza virus. Journal of General Virology 1, 4955.Google Scholar
Rubin, B. A., Pierzchala, W. A. & Neurath, A. R. (1967). Elicitation of antibody response against influenza viruses by different viral subunit preparations. Archiv für die gesamte Virusforschung 20, 268–71.CrossRefGoogle ScholarPubMed
Shelokov, A., Vogel, J. E. & Chi, Lotta (1958). Haemadsorption (adsorption-haemaggluti-nation) test for viral agents in tissue culture with special reference to influenza. Proceedings of the Society for Experimental Biology and Medicine 97, 802–9.Google Scholar
Swanson, P. D., Bradford, H. F. & Mcilwain, H. (1964). Stimulation and solubilization of the sodium ion-activated adenosine triphosphatase of cerebral microsomes by surface-active agents, especially polyoxyethylene ether: actions of phosphatase and neuraminidase. Biochemical Journal 92, 235–47.Google Scholar
Warren, J., Neal, A. & Rennels, D. (1966). Adsorption of myxoviruses on magnetic iron oxides. Proceedings of the Society for Experimental Biology and Medicine 121, 1250–3.Google Scholar
Webster, R. G. & Laver, W. G. (1966). Influenza subunit vaccines: immunogenicity and the loss of toxicity for rabbits of ether and detergent disrupted virus. Journal of Immunology 96, 596605.Google Scholar
Who Expert Committee On Respiratory Virus Diseases (1959). World Health Organization Technical Report Series no. 170, p. 49.Google Scholar