A fluorescent neuraminidase (NA) assay has been developed; 20 samples in five replicates could be analyzed at the same time, allowing us to study the kinetics of the enzyme-substrate interaction. The specificities of six influenza H1N1 virus NAs for BODIPY-labeled 3′SiaLac, 3′SiaLacNAc, SiaLe c , SiaLe a , 6′SiaLac, and 6′SiaLacNAc were evaluated. The duck virus NA hydrolyzed 6′SiaLac and 6′SiaLacNAc 50 times more slowly than 2–3 isomers. Swine viruses digested SiaLe a and 2–6 sialosides 20 times more slowly than 2–3 trisaccharides. For the human viruses, the difference between 2–6 and 2–3 oligosaccharides desialylation efficiency did not exceed five times; notably, the inner core of 2–3 sialosaccharide was discriminated. The results are evidence that influenza virus NAs can distinguish substrate structure at the tri- and tetrasaccharide level.
Archives of Virology – Springer Journals
Published: Oct 1, 2007
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