Skip to main content
Log in

Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus

  • Brief Report
  • Published:
Archives of Virology Aims and scope Submit manuscript

Summary

The acetylesterase of influenza C virus has been reported recently to be inhibited by diisopropylfluorophosphate (DFP) [Muchmore EA, Varki A (1987) Science 236: 1293–1295]. As this inhibitor is known to bind covalently to the serine in the active site of serine esterases, we attempted to determine the serine in the active site of the influenza C acetylesterase. Incubation of purified influenza C virus with3H-DFP resulted in the selective labelling of the influenza C glycoprotein HEF. The labelled glycoprotein was isolated from a SDS-polyacrylamide gel. Following reduction and carboxymethylation, tryptic peptides of HEF were prepared and analyzed by reversed phase HPLC. The peptide containing the3H-DFP was subjected to sequence analysis. The amino acids determined from the NH2-terminus were used to locate the peptide on the HEF polypeptide. Radiosequencing revealed that3H-DFP is attached to amino acid 17 of the tryptic peptide. These results indicate that serine 71 is the active-site serine of the acetylesterase of influenza C virus.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

References

  1. Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA (1981) Amino acid sequence of Escherichia coli alkaline phosphatase. Proc Natl Acad Sci USA 78: 3473–3477

    Google Scholar 

  2. Buonagurio DA, Nakada S, Desselberger U, Krystal M, Palese P (1985) Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates. Virology 146: 221–232

    Google Scholar 

  3. Formanowski F, Meier-Ewert H (1988) Isolation of the influenza C glycoprotein in a soluble form by bromelain digestion. Virus Res 10: 177–192

    Google Scholar 

  4. Herrler G, Compans RW, Meier-Ewert H (1979) A precursor glycoprotein in influenza C virus. Virology 99: 49–56

    Google Scholar 

  5. Herrler G, Nagele A, Meier-Ewert H, Bhown AS, Compans RW (1981) Isolation and structural analysis of influenza C virion glycoproteins. Virology 113: 439–451

    Google Scholar 

  6. Herrler G, Geyer R, Müller H-P, Stirm S, Klenk H-D (1985) Rat α1-macroglobulin inhibits hemagglutination by influenza C virus. Virus Res 2: 183–192

    Google Scholar 

  7. Herrler G, Rott R, Klenk H-D, Müller H-P. Shukla AK, Schauer R (1985) The receptor-destroying enzyme of influenza C virus is neuraminate O-acetylesterase. EMBO J 4: 1503–1506

    Google Scholar 

  8. Herrler G, Klenk H-D (1987) The surface receptor is a major determinant of the cell tropism of influenza C virus. Virology 159: 102–108

    Google Scholar 

  9. Herrler G, Dürkop I, Becht H, Klenk H-D (1988) The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor. J Gen Virol 69: 839–846

    Google Scholar 

  10. Kitame F, Sugawara K, Ohwada K, Homma M (1982) Proteolytic activation of hemolysis and fusion by influenza C virus. Arch Virol 73: 357–361

    Google Scholar 

  11. MacPhee-Quigley K, Taylor P, Taylor S (1985) Primary structure of the catalytic subunits from two molecular forms of acetylcholinesterase. J Biol Chem 260: 12185–12189

    Google Scholar 

  12. Meier-Ewert H, Nagele A, Herrler G, Basak S, Compans RW (1981) Structure of the spike glycoprotein of influenza C virus. In: Nayak D, Fox CD (eds) Genetic variation among influenza A viruses. Academic Press, New York, pp 263–272

    Google Scholar 

  13. Muchmore EA, Varki A (1987) Selective inactivation of influenza C esterase: a probe for detecting 9-O-acetylated sialic acids. Science 236: 1293–1295

    Google Scholar 

  14. Nakada S, Creager RS, Krystal M, Aaronson RP, Palese P (1984) Influenza C virus hemagglutinin: comparison with influenza A and B virus hemagglutinins. J Virol 50: 118–124

    Google Scholar 

  15. Ohuchi M, Ohuchi R, Mifune K (1982) Demonstration of hemolytic and fusion activities of influenza C virus. J Virol 42: 1076–1079

    Google Scholar 

  16. Pfeifer JB, Compans RW (1984) Structure of the infuenza C glycoprotein as determined from cloned DNA. Virus Res 1: 281–296

    Google Scholar 

  17. Rogers GN, Herrler G, Paulson JC, Klenk H-D (1986) Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem 261: 5947–5951

    Google Scholar 

  18. Vlasak R, Krystal M, Nacht M, Palese P (1987) The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying activities. Virology 160: 419–425

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Herrler, G., Multhaup, G., Beyreuther, K. et al. Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus. Archives of Virology 102, 269–274 (1988). https://doi.org/10.1007/BF01310831

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01310831

Keywords

Navigation