Selective inactivation of influenza C esterase: a probe for detecting 9-O-acetylated sialic acids.
The influenza C virus (INF-C) hemagglutinin recognizes 9-O-acetyl-N-acetylneuraminic acid. The same protein contains the receptor-destroying enzyme (RDE), which is a 9-O-acetyl-esterase. The RDE was inactivated by the serine esterase inhibitor di-isopropyl fluorophosphate (DFP). [3H]DFP-labeling localized the active site to the heavy chain of the glycoprotein. DFP did not alter the hemagglutination or fusion properties of the protein, but markedly decreased infectivity of the virus, demonstrating that the RDE is important for primary infection. Finally, DFP-treated INF-C bound specifically and irreversibly to cells expressing 9-O-acetylated sialic acids. This provides a probe for a molecule that was hitherto very difficult to study.
D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D001681:Biological Assay; D006386:Hemagglutination Tests; D009982:Gammainfluenzavirus / Q000187:drug effects / Q000201:enzymology*; D007531:Isoflurophate / Q000378:metabolism / Q000494:pharmacology*; D051379:Mice; D009975:Orthomyxoviridae / Q000201:enzymology*; D011485:Protein Binding; D012794:Sialic Acids / Q000032:analysis*; D014764:Viral Proteins / Q000378:metabolism
D012794:Sialic Acids; D014764:Viral Proteins; C052637:influenza C virus glycoprotein gpII; D007531:Isoflurophate; C025676:9-O-acetyl-N-acetylneuraminic acid