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.
MeSH Terms
Acetylesterase/physiology
Animals
Carboxylic Ester Hydrolases/analysis
Cattle
Mucins/metabolism
Neuraminic Acids/metabolism
Neuraminidase/physiology
Orthomyxoviridae/enzymology
Receptors, Virus/metabolism
alpha-Macroglobulins/metabolism
Chemicals
Mucins
Neuraminic Acids
Receptors, Virus
alpha-Macroglobulins
Carboxylic Ester Hydrolases
Acetylesterase
sialate O-acetylesterase
Neuraminidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Herrler G
Rott R
Klenk H D
Müller H P
Shukla A K
Schauer R
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