| Literature DB >> 17680329 |
L Mochalova1, V Kurova, Y Shtyrya, E Korchagina, A Gambaryan, I Belyanchikov, N Bovin.
Abstract
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.Entities:
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Year: 2007 PMID： 17680329 DOI： 10.1007/s00705-007-1024-z
Source DB: PubMed Journal: Arch Virol ISSN： 0304-8608 Impact factor: 2.574