1887

Abstract

SUMMARY

We previously reported that nucleoproteins (NPs) of human influenza viruses are cleaved in infected cells and, as a result, two forms of NP, uncleaved (mol. wt. 56000) and cleaved (mol. wt. 53000) were accumulated late in infection. Here, we report that NPs of animal influenza viruses of non-human origin (isolated from pigs, equids, seals, whales, birds) exhibited proteolytic resistance in infected cells and did not undergo a change in mol. wt. in the course of infection. The resistance of the animal virus NPs to proteolytic cleavage was shown to be a virus-specific property and not the consequence of a low level of proteolysis in infected cells. Influenza A/H3N2 viruses isolated from swine in Hong Kong in 1976 were found to have a cleavable NP like that of ‘human’ viruses, supporting the hypothesis concerning the ‘human’ origin of these strains. The NP of human influenza virus (A/Aichi/2/68) adapted to an animal host (mouse) retained susceptibility to limited intracellular proteolysis. Thus, NP resistance to cleavage seems to be a stable viral characteristic enabling the NP56→NP53 modification to be used as an indication of the origin of influenza viruses.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-65-6-1127
1984-06-01
2021-10-17
Loading full text...

Full text loading...

/deliver/fulltext/jgv/65/6/JV0650061127.html?itemId=/content/journal/jgv/10.1099/0022-1317-65-6-1127&mimeType=html&fmt=ahah

References

  1. Aliperti G., Schlesinger M. J. 1978; Evidence for an autoprotease activity of Sindbis virus capsid protein. Virology 90:366–369
    [Google Scholar]
  2. Bhatti A. R., Weber J. 1979; Protease of adenovirus type 2: partial characterization. Virology 96:478–485
    [Google Scholar]
  3. Dittmar K. E. J., Brauer D., Scott A., Moelling K. 1980; Polyprotein processing by retrovirus-specific proteases. European Journal of Cell Biology 22:158–164
    [Google Scholar]
  4. Gold K. 1965; Sulfonyl fluorides as inhibitors of esterases. III. Identification of serine as the site of sulfonylation in phenylmethanesulfonyl a-chymotrypsin. Biochemistry 4:897–901
    [Google Scholar]
  5. Huddleston J. A., Brownlee G. G. 1982; The sequence of the nucleoprotein gene of human influenza A virus, strain A/NT/60/68. Nucleic Acids Research 10:1029–1038
    [Google Scholar]
  6. Nakajima K., Nakajima S., Shortridge K. F., Kendal A. P. 1982; Further genetic evidence for maintenance of early Hong-Kong-like influenza A (H3N2) strains in swine until 1976. Virology 116:562–572
    [Google Scholar]
  7. Nakamura K., Homma M. 1981; Protein synthesis in Vero cells abortively infected with influenza B virus. Journal of General Virology 56:199–202
    [Google Scholar]
  8. Palmenberg A. C., Pallansch M. A., Rueckert R. R. 1979; Protease required for processing picomaviral coat protein resides in the viral replicase gene. Journal of Virology 32:770–778
    [Google Scholar]
  9. Pelham H. R. B. 1978; Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic enzyme. European Journal of Biochemistry 85:457–462
    [Google Scholar]
  10. Pelham H. R. B. 1979; Synthesis and proteolytic processing of cowpea mosaic virus proteins in reticulocyte lysates. Virology 96:463–477
    [Google Scholar]
  11. Schoellmann G., Shaw E. 1963; Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry 2:252–255
    [Google Scholar]
  12. Scupham R. K., Jones K. J., Sagik B. P., Bose H. R. 1977; Virus-directed post-translational cleavage in Sindbis virus-infected cells. Journal of Virology 22:568–571
    [Google Scholar]
  13. Shaw E., Mares-Guia M., Cohen W. 1965; Evidence for an active-center histidine in trypsin through use of a specific reagent, l-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from N-a- tosyl-L-lysine. Biochemistry 4:2219–2224
    [Google Scholar]
  14. Shortridge K. F., Cherry A., Kendal A. P. 1979; Further studies of the antigenic properties of H3N2 strains of influenza A isolated from swine in South East Asia. Journal of General Virology 44:251–254
    [Google Scholar]
  15. Trautschold I., Werle E., Zickgraf-Rudel G. 1967; Trasylol. Biochemical Pharmacology 16:59–72
    [Google Scholar]
  16. Von Der Helm K. 1977; Cleavage of Rous sarcoma viral polypeptide precursor into internal structural proteins in vitro involves viral protein pl5. Proceedings of the National Academy of Sciences, U. S. A 74:911–915
    [Google Scholar]
  17. Webster R., Laver W. G. 1975; Antigenic variation of influenza viruses. In The Influenza Viruses and Influenza pp. 269–314 Edited by Kilbourne E. D. New York: Academic Press;
    [Google Scholar]
  18. Winter G., Fields S. 1981; The structure of the gene encoding the nucleoprotein of human influenza virus A/PR/8/34. Virology 114:423–428
    [Google Scholar]
  19. Zhirnov O. P., Bukrinskaya A. G. 1981; Two forms of influenza virus nucleoprotein in infected cells and virions. Virology 109:174–179
    [Google Scholar]
  20. Zhirnov O. P., Ovcharenko A. V., Bukrinskaya A. G. 1982a; A modified plaque assay method for accurate analysis of infectivity of influenza viruses with uncleaved hemagglutinin. Archives of Virology 71:177–183
    [Google Scholar]
  21. Zhirnov O. P., Ovcharenko A. V., Bukrinskaya A. G. 1982b; Protective effect of protease inhibitors in influenza virus infected animals. Archives of Virology 73:263–272
    [Google Scholar]
  22. Zhirnov O. P., Ovcharenko A. V., Bukrinskaya A. G. 1984; Suppression of influenza virus replication in infected mice by protease inhibitors. Journal of General Virology 65:191–196
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-65-6-1127
Loading
/content/journal/jgv/10.1099/0022-1317-65-6-1127
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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