Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Oct;64(2):634–641. doi: 10.1073/pnas.64.2.634

THE RELATIONSHIP OF THE INFLUENZA VIRUS INHIBITORY ACTIVITY OF GLYCOPROTEINS TO THEIR MOLECULAR SIZE AND SIALIC ACID CONTENT

Georg F Springer 1,2, H Gerhard Schwick 1,2, Mary Ann Fletcher 1,2
PMCID: PMC223391  PMID: 5261039

Abstract

Twenty-four different glycoproteins were investigated for their ability to inhibit hemagglutination by the A/PRS and the B/Md influenza virus strains. A relationship between activity, the molecular size, and sialic acid content was found. This relationship was readily shown for the A/PR8 virus if the properties of the glycoproteins were compared with one another on a per cent basis. A proportion of approximately 1:1:1 for activity (weight basis) to moles sialic acid content to molecular weight existed for each inhibitory glycoprotein with more than 3 per cent sialic acid, on comparison with any other active glycoprotein.

A 1:3 correspondence between viral subunit and sialic acid residues of the inhibitor ovine submaxillary mucin was found experimentally and confirmed by calculation on a molecular model. The most potent inhibitors, were the antigens of the human blood-group MN system and the Tamm-Horsfall urinary glycoprotein.

Full text

PDF
634

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Almeida J. D., Waterson A. P. Some observations on the envelope of an influenza virus. J Gen Microbiol. 1967 Jan;46(1):107–110. doi: 10.1099/00221287-46-1-107. [DOI] [PubMed] [Google Scholar]
  2. BARRY G. T., GOEBEL W. F. Colominic acid, a substance of bacterial origin related to sialic acid. Nature. 1957 Jan 26;179(4552):206–206. doi: 10.1038/179206a0. [DOI] [PubMed] [Google Scholar]
  3. CONNELL G. E., DIXON G. H., SMITHIES O. Subdivision of the three common haptoglobin types based on 'hidden' diffrences. Nature. 1962 Feb 3;193:505–506. doi: 10.1038/193505a0. [DOI] [PubMed] [Google Scholar]
  4. Hirst G. K. THE AGGLUTINATION OF RED CELLS BY ALLANTOIC FLUID OF CHICK EMBRYOS INFECTED WITH INFLUENZA VIRUS. Science. 1941 Jul 4;94(2427):22–23. doi: 10.1126/science.94.2427.22. [DOI] [PubMed] [Google Scholar]
  5. Horowitz M. I., Das A. Immunochemistry of ovine and bovine submaxillary mucins. Immunochemistry. 1967 Sep;4(5):303–313. doi: 10.1016/0019-2791(67)90113-9. [DOI] [PubMed] [Google Scholar]
  6. KATHAN R. H., WINZLER R. J., JOHNSOM C. A. Preparation of an inhibitor of viral hemagglutination from human erythrocytes. J Exp Med. 1961 Jan 1;113:37–45. doi: 10.1084/jem.113.1.37. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KLENK E., UHLENBRUCK G. [On the isolation of mucoids containing neuraminic acid from human erythrocyte stroma, a contribution to the chemistry of agglutinogens]. Hoppe Seylers Z Physiol Chem. 1960;319:151–160. doi: 10.1515/bchm2.1960.319.1.151. [DOI] [PubMed] [Google Scholar]
  8. LAURELL A. B. Inhibitor capacity of some purified human serum proteins on hemagglutination by influenza virus. Acta Pathol Microbiol Scand. 1960;49:213–222. doi: 10.1111/j.1699-0463.1960.tb01132.x. [DOI] [PubMed] [Google Scholar]
  9. MCGUIRE E. J., BINKLEY S. B. THE STRUCTURE AND CHEMISTRY OF COLOMINIC ACID. Biochemistry. 1964 Feb;3:247–251. doi: 10.1021/bi00890a017. [DOI] [PubMed] [Google Scholar]
  10. ODIN L. Carbohydrate residue of a urine mucoprotein inhibiting influenza virus hemagglutination. Nature. 1952 Oct 18;170(4329):663–664. doi: 10.1038/170663a0. [DOI] [PubMed] [Google Scholar]
  11. PUSZTAI A., MORGAN W. T. Studies in immunochemistry. 18. The isolation and properties of a sialomucopolysaccharide possessing blood-group Le-a specificity and virus-receptor activity. Biochem J. 1961 Jan;78:135–146. doi: 10.1042/bj0780135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Springer G. F., Ansell N. J. INACTIVATION OF HUMAN ERYTHROCYTE AGGLUTINOGENS M AND N BY INFLUENZA VIRUSES AND RECEPTOR-DESTROYING ENZYME. Proc Natl Acad Sci U S A. 1958 Feb;44(2):182–189. doi: 10.1073/pnas.44.2.182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Springer G. F. Human MN glycoproteins: dependence of blood-group and anti-influenza virus activities on their molecular size. Biochem Biophys Res Commun. 1967 Aug 23;28(4):510–513. doi: 10.1016/0006-291x(67)90342-7. [DOI] [PubMed] [Google Scholar]
  14. TAKATSY G. The use of spiral loops in serological and virological micro-methods. Acta Microbiol Acad Sci Hung. 1955;3(1-2):191–202. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES