Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-23T22:22:16.358Z Has data issue: false hasContentIssue false
  • English
  • Français

Structure of the influenza virus. The relation between biological activity and chemical structure of virus fractions

Published online by Cambridge University Press:  15 May 2009

L. Hoyle
L. Hoyle
Affiliation:
Public Health Laboratory (Medical Research Council), Northampton
Rights & Permissions [Opens in a new window]

Extract

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.

Influenza virus elementary bodies can be disintegrated by treatment with ether with the liberation of two types of smaller particle, soluble antigen and red cell agglutinin.

Soluble antigen derived from the elementary body is identical in serological and chemical behaviour with soluble antigen recovered from infected tissues. Its chemical properties are those of a ribonucleoprotein.

The agglutinin is an enzyme, with a protein part carrying the enzymic activity and a combining group with affinity for red cells. The agglutinin does not react in complement-fixation tests by the short fixation technique, but by the use of prolonged fixation or by indirect complement fixation it can be shown to contain a strain specific antigen and also a non-specific antigen. The specific antigen is identical with the specific complement-fixing antigen demonstrable in the intact elementary body, and has combining affinity for red blood cells. The non-specific antigen is probably similar to the protein part of the soluble antigen. No evidence has been found that the agglutinin contains either carbohydrate or nucleic acid.

From the ether used to disintegrate the elementary body a serologically active lipid can be recovered which has properties suggesting that it is derived from the host cell.

The author is greatly indebted to Dr L. Dmochowski for assistance in experiments involving high-speed centrifugation, to Sir Macfarlane Burnet and Dr G. L. Ada for supplies of receptor-destroying enzyme, to Dr E. S. Duthie for crystalline trypsin and chymotrypsin, and to Dr R. R. Porter for a sample of crystalline ribonuclease.

Type
Research Article
Information
Journal of Hygiene , Volume 50 , Issue 2 , June 1952 , pp. 229 - 245
Copyright
Copyright © Cambridge University Press 1952

References

REFERENCES

Anderson, S. C. (1947). Aust. J. Sci. 10, 83.Google Scholar
Burnet, F. M. & Lind, P. E. (1951). J. gen. Microbiol. 5, 67.CrossRefGoogle Scholar
Fazekas De St Groth, S. & Graham, D. M. (1949). Aust. J. exp. Biol. med. Sci. 27, 83.CrossRefGoogle Scholar
Graham, A. F. (1950). Canad. J. Res. 28, 186.CrossRefGoogle Scholar
Henle, W. & Wiener, M. (1944). Proc. Soc. exp. Biol., N.Y., 57, 176.CrossRefGoogle Scholar
Hirst, G. K. (1948). J. exp. Med. 89, 315.CrossRefGoogle Scholar
Hirst, G. K. (1949). J. exp. Med. 89, 233.CrossRefGoogle Scholar
Hoyle, L. (1945). J. Hyg., Camb., 44, 170.CrossRefGoogle Scholar
Hoyle, L. (1948). Brit. J. exp. Path. 29, 390.Google Scholar
Hoyle, L. (1950). J. Hyg., Camb., 48, 277.CrossRefGoogle Scholar
Hoyle, L. & Fairbrother, R. W. (1937). J. Hyg., Camb., 37, 512.Google Scholar
Hoyle, L., Reed, R. & Astbury, W. T. (1952). (In the Press.)Google Scholar
Knight, C. A. (1946). J. exp. Med. 83, 281.CrossRefGoogle Scholar
Knight, C. A. (1947). J. exp. Med. 85, 99.CrossRefGoogle Scholar
Northrop, J. H., Kunitz, M. & Herriot, R. M. (1948). Crystalline Enzymes, p. 232. Columbia University Press.Google Scholar
Stone, J. D. (1949). Aust. J. exp. Biol. med. Sci. 27, 337.CrossRefGoogle Scholar