Skip to main content
The EMBO Journal logoLink to The EMBO Journal
. 1985 Jun;4(6):1503–1506. doi: 10.1002/j.1460-2075.1985.tb03809.x

The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase.

G Herrler, R Rott, H D Klenk, H P Müller, A K Shukla, R Schauer
PMCID: PMC554374  PMID: 2411539

Abstract

The nature of the receptor-destroying enzyme (RDE) of influenza C virus has been elucidated by analyzing its effect on the haemagglutination inhibitors rat alpha 1-macroglobulin (RMG) and bovine submandibulary mucin (BSM), respectively. The inhibitory activity of both compounds is abolished by incubation with influenza C virus. After inactivation, RMG and BSM were found to contain reduced amounts of N-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) and increased amounts of N-acetylneuraminic acid (Neu5Ac). H.p.l.c. analysis revealed that purified Neu5,9Ac2 is converted to Neu5Ac by incubation with influenza C virus. These results demonstrate that RDE of influenza C virus is neuraminate-O-acetylesterase [N-acyl-9(4)-O-acetylneuraminate O-acetylhydrolase (EC 3.1.1.53)]. The data also indicate that haemagglutination-inhibition (HI) by RMG and BSM and most likely virus attachment to cell surfaces involves binding of influenza C virus to Neu5,9Ac2.

Full text

PDF
1503

Images in this article

Selected References

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

  1. Buscher H. P., Casals-Stenzel J., Schaufer R. New sialic acids. Identification of N-glycoloyl-O-acetylneuraminic acids and N-acetyl-O-glycoloylneuraminic acids by improved methods for detection of N-acyl and O-acyl groups and by gas-liquid chromatography. Eur J Biochem. 1974 Dec 16;50(1):71–82. doi: 10.1111/j.1432-1033.1974.tb03873.x. [DOI] [PubMed] [Google Scholar]
  2. Chucholowius H. W., Rott R. A new method for purification of myxoviruses by zonal centrifugation with two different sucrose density gradients. Proc Soc Exp Biol Med. 1972 May;140(1):245–247. doi: 10.3181/00379727-140-36434. [DOI] [PubMed] [Google Scholar]
  3. GOTTSCHALK A. Neuraminidase: the specific enzyme of influenza virus and Vibrio cholerae. Biochim Biophys Acta. 1957 Mar;23(3):645–646. doi: 10.1016/0006-3002(57)90389-x. [DOI] [PubMed] [Google Scholar]
  4. HIRST G. K. The relationship of the receptors of a new strain of virus to those of the mumps-NDV-influenza group. J Exp Med. 1950 Feb;91(2):177–184. doi: 10.1084/jem.91.2.177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Haverkamp J., Schauer R., Wember M., Kamerling J. P., Vliegenthart J. F. Synthesis of 9-O-acetyl- and 4,9-di-O-acetyl derivatives of the methyl ester of N-acetyl-beta-D-neuraminic acid methylglycoside. Their use as models in periodate oxidation studies. Hoppe Seylers Z Physiol Chem. 1975 Oct;356(10):1575–1583. doi: 10.1515/bchm2.1975.356.2.1575. [DOI] [PubMed] [Google Scholar]
  6. Herrler G., Compans R. W., Meier-Ewert H. A precursor glycoprotein in influenza C virus. Virology. 1979 Nov;99(1):49–56. doi: 10.1016/0042-6822(79)90035-7. [DOI] [PubMed] [Google Scholar]
  7. Herrler G., Geyer R., Müller H. P., Stirm S., Klenk H. D. Rat alpha 1 macroglobulin inhibits hemagglutination by influenza C virus. Virus Res. 1985 Mar;2(2):183–192. doi: 10.1016/0168-1702(85)90248-5. [DOI] [PubMed] [Google Scholar]
  8. Herrler G., Rott R., Klenk H. D. Neuraminic acid is involved in the binding of influenza C virus to erythrocytes. Virology. 1985 Feb;141(1):144–147. doi: 10.1016/0042-6822(85)90190-4. [DOI] [PubMed] [Google Scholar]
  9. KLENK E., FAILLARD H., LEMPFRID H. Uber die enzymatische Wirkung von Influenzavirus. Hoppe Seylers Z Physiol Chem. 1955 Sep 2;301(4-6):235–246. [PubMed] [Google Scholar]
  10. Kamerling J. P., Makovitzky J., Schauer R., Vliegenthart J. F., Wember M. The nature of sialic acids in human lymphocytes. Biochim Biophys Acta. 1982 Feb 2;714(2):351–355. doi: 10.1016/0304-4165(82)90344-0. [DOI] [PubMed] [Google Scholar]
  11. Kendal A. P. A comparison of "influenza C" with prototype myxoviruses: receptor-destroycing activity (neuraminidase) and structural polypeptides. Virology. 1975 May;65(1):87–99. doi: 10.1016/0042-6822(75)90009-4. [DOI] [PubMed] [Google Scholar]
  12. Ohuchi M., Homma M., Muramatsu M., Ohyama S. Properties of the erythrocyte receptors for influenza C virus. Microbiol Immunol. 1978;22(4):197–203. doi: 10.1111/j.1348-0421.1978.tb00363.x. [DOI] [PubMed] [Google Scholar]
  13. Pepper D. S. The sialic acids of horse serum with special reference to their virus inhibitory properties. Biochim Biophys Acta. 1968 Mar 11;156(2):317–326. doi: 10.1016/0304-4165(68)90261-4. [DOI] [PubMed] [Google Scholar]
  14. Schauer R. Characterization of sialic acids. Methods Enzymol. 1978;50:64–89. doi: 10.1016/0076-6879(78)50008-6. [DOI] [PubMed] [Google Scholar]
  15. Schauer R. Chemistry, metabolism, and biological functions of sialic acids. Adv Carbohydr Chem Biochem. 1982;40:131–234. doi: 10.1016/s0065-2318(08)60109-2. [DOI] [PubMed] [Google Scholar]

Articles from The EMBO Journal are provided here courtesy of Nature Publishing Group

RESOURCES