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The chemical reactions of the haemagglutinins and neuraminidases of different strains of influenza viruses: I. Effect of reagents reacting with amino acids in the active centres

Published online by Cambridge University Press:  15 May 2009

L. Hoyle
Affiliation:
Public Health Laboratory, Northampton
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Summary

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Studies of the chemical reactions of the haemagglutinins and neuraminidases of eight strains of influenza viruses have been made by the use of chemical reagents reacting with chemically active groups in the protein molecule. The results indicate a close resemblance between the active centres of the haemagglutinins and neuraminidases in all the strains tested. In all cases the activities were unaffected by reagents reacting with the —SH group of cysteine, the —CH3S group of methionine, the amino group of lysine, the guanidyl group of arginine, or the indole ring of tryptophan. In all cases both the haemagglutinating and enzymic activities were reduced or destroyed by agents reacting with amide groups or reacting with both tyrosine and histidine.

By the use of iodine under conditions in which tyrosine reacts but not histidine, and fluorodinitrobenzene under conditions in which histidine reacts more strongly than tyrosine, it was possible to detect a number of different active centres.

(1) An active centre containing histidine and an amide group but not containing tyrosine was present in all the virus strains and was the only centre detectable in A1 and A2 strains. This type of centre appeared to possess both haemagglutinating and neuraminidase activity.

(2) Active centres containing tyrosine and an amide group were detected in strains of A and B viruses. There was some evidence suggesting that tyrosine-containing centres were of two types: one possessing both haemagglutinating and enzymic activity while the other was a haemagglutinin without neuraminidase activity.

The results could be explained by supposing that the presence of histidine in the active centre was essential for neuraminidase activity and that enzymically active tyrosine-containing centres also contained histidine, but that tyrosine could substitute for histidine, but that tyrosine could substitute for histidine in haemagglutinating centres.

Type
Research Article
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
Fraenkel-Conrat, H. & Olcott, H. S. (1948). The reaction of formaldehyde with proteins. Cross linking between amino and primary amide or guanidyl groups. J. Am. chem. Soc. 70, 2673.CrossRefGoogle ScholarPubMed
Hoyle, L. (1969). 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. J. Hyg., Camb. 67, 301.CrossRefGoogle ScholarPubMed
Hoyle, L. & Hana, L. (1966). The chemical reactions of influenza virus proteins. J. Path. Bact. 92, 447–60.CrossRefGoogle ScholarPubMed
McKinney, L. L., Uhing, E. H., Setzkorn, E. A. & Cowan, J. C. (1950). Cyanoethylation of α-amino acids. I. Monocyanoethyl derivatives. J. Am. chem. Soc. 72, 2599–603.CrossRefGoogle Scholar
Nakaya, K., Horinishi, H. & Shibata, K. (1967). States of amino acid residues in protein. XIV. Glyoxal as a reagent for discrimination of arginine residues. J. Biochem., Tokyo 61, 345–51.CrossRefGoogle ScholarPubMed