MOCHALOVA L, Kurova V, Shtyrya Y, Korchagina E, et. Oligosaccharide specificity of influenza H1N1 virus neuraminidases. Arch Virol. 2007 Aug 6
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.
See Also:
- http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=17680329&dopt=AbstractPlus
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