1887

Abstract

SUMMARY: Antisera were prepared to several strains of influenza virus (grown in the chick embryo), to purified neuraminidase and to partially purified neuraminidase from chick chorioallantois. The ability of the antisera to inhibit the action of each enzyme on substrates of different molecular weight was tested. The substrates used and their molecular weights were sialyl lactose (640), fetuin (48,000) and ovine submaxillary gland mucin, OSM (1 × 10). Antiserum to and avian neuraminidase inhibited strongly the action of the homologous enzyme on each substrate. Antiserum to viral neuraminidase inhibited almost completely homologous action on fetuin and OSM but only partially the action on sialyl lactose. LEE influenza virus was grown in embryonated eggs and in cultures of calf kidney cells and from each preparation a soluble neuraminidase was isolated. Antiserum to the egg-grown virus inhibited the enzyme of both viruses not only in the intact virus particle, but also after separation in the form of a soluble, low molecular weight product. There was little or no serological cross-reaction between any enzyme and heterologous antisera, with one exception. Antiserum to avian neuraminidase partially inhibited (fetuin, but not sialyl lactose, as substrate) the soluble enzyme derived from egg-grown LEE virus, but not from virus grown in cultures of calf kidney cells. It was concluded that the soluble enzyme prepared from LEE virus is a virus specific product but also carries some antigenic determinants characteristic of host specificity.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-32-2-225
1963-08-01
2024-12-12
Loading full text...

Full text loading...

/deliver/fulltext/micro/32/2/mic-32-2-225.html?itemId=/content/journal/micro/10.1099/00221287-32-2-225&mimeType=html&fmt=ahah

References

  1. Ada G. L., Lind P. E. 1961; Neuraminidase in the chorioallantois of the chick embryo. Nature, Lond 190:1169
    [Google Scholar]
  2. Ada G. L. 1963; Purification and properties of avian neuraminidase. Biochim. biophys. Acta (in the press)
    [Google Scholar]
  3. Ada G. L., French E. L., Lind P. E. 1961; Purification and properties of neuraminidase from Vibrio cholerae. J. gen. Microbiol 24:409
    [Google Scholar]
  4. Aronsson T., Grönwall A. 1957; Improved separation of serum proteins in paper electrophoresis. A new electrophoresis buffer. Scand. J. clin. lab. Invest 9:338
    [Google Scholar]
  5. Burnet F. M., Beveridge W. I. B., Bull D. R., Clarke E. 1942; Investigations of an influenza epidemic in military camps in Victoria, May, 1942. Med. J. Austral ii:371
    [Google Scholar]
  6. Beveridge W. I. B., Burnet F. M. 1946; The cultivation of viruses and rickettsiae in the chick embryo. Spec. Rep. Ser. med. Res. Counc., Lond no. 256 London: H.M. Stationery Office;
    [Google Scholar]
  7. Carubelli R., Trucco R. E., Caputto R. 1962; Neuraminidase activity in mammalian organs. Biochim. biophys. Acta 60:196
    [Google Scholar]
  8. Cinader B. 1957; Antibodies against enzymes. Annu. Rev. Microbiol 11:371
    [Google Scholar]
  9. Francis T. 1934; Transmission of influenza by filterable virus. Science 80:457
    [Google Scholar]
  10. Francis T. 1940; New type of virus from epidemic influenza. Science 92:405
    [Google Scholar]
  11. Gottschalk A., McKenzie H. A. 1961; Studies on mucoproteins. VIII. On the molecular size and shape of ovine submaxillary gland mucoprotein. Biochim. biophys. Acta 54:226
    [Google Scholar]
  12. Laver W. G. 1962; The structure of influenza viruses. 1. N-Terminal amino acid analyses. Virology 18:19
    [Google Scholar]
  13. Laver W. G. 1963a; The structure of influenza viruses. 2. C-terminal amino acid analyses. Virology (in the press)
    [Google Scholar]
  14. Laver W. G. 1963b; The structure of influenza viruses. 3. Separation of neuraminidase activity after disruption of an influenza virus with detergents. Virology (in the press)
    [Google Scholar]
  15. McCrea J. F., Epstein R. S., Barry W. H. 1961; Use of potassium tartrate for equilibrium density-gradient centrifugation of animal viruses. Nature, Lond 189:220
    [Google Scholar]
  16. Pollock M. R. 1956; An immunological study of the constitutive and the penicillin-induced penicillinases of Bacillus cereus, based on specific enzyme neutralization by antibody. J. gen. Microbiol 14:90
    [Google Scholar]
/content/journal/micro/10.1099/00221287-32-2-225
Loading
/content/journal/micro/10.1099/00221287-32-2-225
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error