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Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function

1989; American Society for Microbiology; Volume: 63; Issue: 5 Linguagem: Inglês

10.1128/jvi.63.5.2056-2062.1989

1098-5514

Reinhard Vlasak, Thomas Muster, Andrea Marie Lauro, James C. Powers, Peter Palese,

Influenza Virus Research Studies

The active site serine of the acetylesterase of influenza C virus was localized to amino acid 71 of the hemagglutinin-esterase protein by affinity labeling with 3H-labeled diisopropylfluorophosphate. This serine and the adjacent amino acids (Phe-Gly-Asp-Ser) are part of a consensus sequence motif found in serine hydrolases. Since comparative analysis failed to reveal esterase sequence similarities with other serine hydrolases, we suggest that this viral enzyme is a serine hydrolase constituting a new family of serine esterases. Furthermore, we found that the influenza C virus esterase was inhibited by isocoumarin derivatives, with 3,4-dichloroisocoumarin being the most potent inhibitor. Addition of this compound prevented elution of influenza C virus from erythrocytes and inhibited virus infectivity, possibly through inhibition of virus entry into cells.