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The chemical reactions of the haemagglutinins and neuraminidases of different strains of influenza viruses: II. Effects of reagents modifying the higher order structure of the protein molecule

Published online by Cambridge University Press:  15 May 2009

L. Hoyle
L. Hoyle
Affiliation:
Public Health Laboratory, Northampton
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Summary

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The results of treatment of influenza virus strains with chemical reagents acting on the higher-order structure of protein molecules shows that both the haemagglutinating and enzymic activities are susceptible to these agents but there are considerable differences between the different strains and the neuraminidase activity is more sensitive than the haemagglutinating activity.

The neuraminidase activity of A and A1 strains is destroyed by urea, guanidine, urea+dithiothreitol and mercuric chloride. The haemagglutinin of the PR 8 and SWINE strains is resistant to urea and mercuric chloride but destroyed by guanidine and by urea+dithiothreitol. The haemagglutinin of the DSP strain of virus A and the A1 strains is resistant to urea, guanidine and mercuric chloride but is destroyed by urea+dithiothreitol.

The neuraminidase activity of the A2 strains is more resistant than that of the A and A1 strains. It is resistant to mercuric chloride and partially resistant to urea but is destroyed by guanidine and by urea+dithiothreitol. The A2 haemagglutinin is resistant to urea, urea+dithiothreitol, and mercuric chloride but is destroyed by guanidine.

The LEE virus neuraminidase is resistant to urea and partially resistant to guanidine but is destroyed by urea+dithiothreitol and mercuric chloride. The LEE haemagglutinin is resistant to urea, guanidine and mercuric chloride but is destroyed by urea+dithiothreitol.

It is suggested that the surface projections of the virus particle are protein polymers each made up of three or four monomers which are the components of the V antigen complex. Antigenic activity is a function of the primary or secondary structure of the monomers, haemagglutinin activity is a function of the tertiary structure of the monomers, while neuraminidase activity is a function of the quaternary structure of the polymer.

From studies of the chemical reactions of their haemagglutinins and neuraminidases strains of influenza virus A can be classified into groups. These groups are very similar to but not precisely identical with groupings made by serological methods.

Type
Research Article
Information
Journal of Hygiene , Volume 67 , Issue 2 , June 1969 , pp. 301 - 310
Copyright
Copyright © Cambridge University Press 1969

References

REFERENCES

Aminoff, D. (1961). Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem. J. 81, 384–92.CrossRefGoogle ScholarPubMed
Cleland, W. W. (1964). Dithiothreitol, a new protective reagent for SH groups. Biochemistry 3, 480–2.CrossRefGoogle ScholarPubMed
Drzeniek, R., Seto, J. T. & Rott, R. (1966). Characterisation of neuraminidases from myxoviruses. Biochim. biophys. Acta 128, 547–58.CrossRefGoogle Scholar
Eckert, E. A. (1966 a). Envelope proteins derived from influenza virus. J. Bact. 91, 1907–10.CrossRefGoogle ScholarPubMed
Eckert, E. A. (1966 b). Characterization of a low molecular weight antigenic protein from the envelope of influenza virus. J. Bact. 92, 1430–4.CrossRefGoogle ScholarPubMed
Eckert, E. A. (1967). Envelope protein of influenza virus. I. Haemagglutinating activity of reassociated sub-units. J. Virol. 1, 920–7.CrossRefGoogle Scholar
Hobson, D. (1966). The strain-specific serological activity of a non-haemagglutinating fraction of influenza viruses. Br. J. exp. Path. 47, 257–65.Google Scholar
Hoyle, L. (1969). The chemical reactions of the haemagglutinins and neuraminidases of different strains of influenza viruses. I. J. Hyg., Camb. 67, 289.CrossRefGoogle ScholarPubMed
Hoyle, L. & Hana, L. (1966). The chemical reaction of influenza virus proteins. J. Path. Bact. 92, 447–60.CrossRefGoogle ScholarPubMed
Jagger, J. & Pollard, E. C. (1956). Inactivation with fast charged particles of infectivity and haemagglutination in influenza A virus. Radiat. Res. 4, 1–19.CrossRefGoogle ScholarPubMed
Laver, W. G. (1963). The structure of influenza viruses. 3. Disruption of the virus particle and separation of neuraminidase activity. Virology 20, 251–62.CrossRefGoogle Scholar
Laver, W. G. & Kilbourne, E. D. (1966). Identification in a recombinant influenza virus of structural proteins derived from both parents. Virology 30, 493–501.CrossRefGoogle Scholar
Mayron, L. W., Robert, B., Winzler, R. J. & Rafaelson, M. E. (1961). Studies on the neuraminidases of influenza virus. 1. Separation and some properties of the enzyme from Asian and PR 8 strains. Archs Biochem. Biophys. 92, 475–83.CrossRefGoogle Scholar
Noll, H., Aoyagi, T. & Orlando, J. (1962). The structural relationship of sialidase to the influenza virus surface. Virology 18, 154–7.CrossRefGoogle Scholar
Paniker, C. K. J. (1968). Serological relationships between the neuraminidases of influenza viruses. J. gen. Virol. 2, 385–94.CrossRefGoogle ScholarPubMed
Rafaelson, M. E., Wilson, V. W. & Schneir, M. (1962). The neuraminidases of influenza virus. Med. Bull. Presb. St Luke's Hosp. 1, 34–9.Google Scholar
Reginster, M. (1966 a). Release of influenza virus neuraminidase by caseinase C of Streptomyces albus G. J. gen. Microbiol. 42, 323–31.CrossRefGoogle ScholarPubMed
Reginster, M. (1966 b). Effects of pronase on influenza virus. Acta virol. Prague 10, 111–16.Google ScholarPubMed
Reginster, M. (1968). Recherches sur la structure du virus grippal. Mém. Soc. r. Sci. Liège 16, fasc. 4.Google Scholar
Seto, J. T., Drzeniek, R. & Rott, R. (1966). Isolation of a low molecular weight sialidase (neuraminidase) from influenza virus. Biochim. biophys. Acta 113, 402–4.CrossRefGoogle Scholar