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Antigenic structure of influenza viruses; the preparation of elementary body suspensions and the nature of the complement-fixing antigen

Published online by Cambridge University Press:  15 May 2009

Leslie Hoyle  and
R. W. Fairbrother
Leslie Hoyle
Affiliation:
From the Department of Bacteriology and Preventive Medicine, University of Manchester
R. W. Fairbrother
Affiliation:
From the Department of Bacteriology and Preventive Medicine, University of Manchester
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There is much evidence to indicate that viruses, in certain cases at least, have an antigenic structure of comparable complexity to that of the bacteria. Hughes (1933) found that the serum of animals immunized with the yellow-fever virus contained two independent antibodies—precipitins and protective antibodies; the precipitinogen was distinct from the virus. Craigie & Wishart (1936) in investigations of the vaccinia virus have shown that, in addition to the elementary bodies, virus suspensions contain two soluble precipitable substances, the “L” antigen which is labile at 56° C. and the “S” antigen which is stable at 95° C. These antigens were readily demonstrated by precipitation, agglutination and complement fixation. Their nature and origin have not, however, been precisely determined. Bedson (1936), working with the psittacosis virus, prepared a soluble antigen, which was independent of the elementary bodies. It was most satisfactorily demonstrated by complement fixation.

Type
Research Article
Information
Journal of Hygiene , Volume 37 , Issue 4 , October 1937 , pp. 512 - 520
Copyright
Copyright © Cambridge University Press 1937

References

Bedson, S. P. (1936). Brit. J. Exp. Path. 17, 109.Google Scholar
Craigie, J. & Wishart, F. O. (1936). J. Exp. Med. 64, 803.CrossRefGoogle Scholar
Eagles, G. H. & Ledingham, J. C. G. (1932). Lancet, i, 832.Google Scholar
Elford, W. J.Andrewes, C. H. & Tang, F. T. (1936). Brit. J. Exp. Path. 17, 51.Google Scholar
Fairbrother, R. W. & Hoyle, L. (1937). J. Path. Bact. 44, 213.CrossRefGoogle Scholar
Hoyle, L. & Fairbrother, R. W. (1937). Brit. Med. J. 1, 655.Google Scholar
Hughes, T. P. (1933). J. Immunol. 25, 275.CrossRefGoogle Scholar
Laidlaw, P. P.Andrewes, C. H.Smith, W. & Dunkin, G. W. (1935). Brit. J. Exp. Path. 16, 275.Google Scholar
Smith, W. (1936). Lancet, ii, 1256.Google Scholar