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. 1989 May;63(5):2056–2062. doi: 10.1128/jvi.63.5.2056-2062.1989

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

R Vlasak 1, T Muster 1, A M Lauro 1, J C Powers 1, P Palese 1
PMCID: PMC250621  PMID: 2495370

Abstract

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.

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Selected References

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