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Characterization of the receptor-destroying enzyme activity from infectious salmon anaemia virus

Department of Microbiology, School of Pharmacy, PO Box 1068, Blindern, 0316 Oslo, Norway¹

Author for correspondence: Tor Gjøen. Fax +47 22844944. e-mail tor.gjoen{at}farmasi.uio.no

Infectious salmon anaemia virus (ISAV) infects cells via the endocytic pathway and, like many other enveloped viruses, ISAV contains a receptor-destroying enzyme. We have analysed this acetylesterase activity with respect to substrate specificity, enzyme kinetics, inhibitors, temperature and pH stability. The ISAV acetylesterase was inhibited by di-isopropyl fluorophosphate (DFP) in a dose-dependent fashion but not by other known hydrolase inhibitors, suggesting that a serine residue is part of the active site. The pH optimum of the enzyme was in the range 7·5–8·0 and the enzymatic activity was lessened at temperatures above 40 °C. The effect of DFP on agglutination/elution of erythrocytes by ISAV demonstrated that the acetylesterase activity is the bona fide receptor-destroying enzyme. A haemadsorption assay was used to analyse whether the esterase was active on the surface of infected cells or not.

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