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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  and
P. H. Gallimore
N. M. Larin
Affiliation:
Research Division, Pfizer Limited, Sandwich, Kent
P. H. Gallimore
Affiliation:
Research Division, Pfizer Limited, Sandwich, Kent
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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
Information
Journal of Hygiene , Volume 69 , Issue 1 , March 1971 , pp. 35 - 46
Copyright
Copyright © Cambridge University Press 1971

References

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