4-4-difluoro-4-bora-3a-4a-diaza-s-indacene and Influenza--Human

4-4-difluoro-4-bora-3a-4a-diaza-s-indacene has been researched along with Influenza--Human* in 1 studies

Other Studies

1 other study(ies) available for 4-4-difluoro-4-bora-3a-4a-diaza-s-indacene and Influenza--Human

Article	Year
Oligosaccharide specificity of influenza H1N1 virus neuraminidases. Archives of virology, 2007, Volume: 152, Issue:11 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. Topics: Animals; Boron Compounds; Ducks; Fluorescent Dyes; Humans; Influenza A Virus, H1N1 Subtype; Influenza in Birds; Influenza, Human; Kinetics; Neuraminidase; Oligosaccharides; Orthomyxoviridae Infections; Substrate Specificity; Swine	2007

Article

Year

Oligosaccharide specificity of influenza H1N1 virus neuraminidases.

Archives of virology, 2007, Volume: 152, Issue:11

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.

Topics: Animals; Boron Compounds; Ducks; Fluorescent Dyes; Humans; Influenza A Virus, H1N1 Subtype; Influenza in Birds; Influenza, Human; Kinetics; Neuraminidase; Oligosaccharides; Orthomyxoviridae Infections; Substrate Specificity; Swine

2007