Determination of neuraminidase kinetic constants using whole influenza virus preparations and correction for spectroscopic interference by a fluorogenic substrate

The influenza neuraminidase (NA) enzyme cleaves terminal sialic acid residues from cellular receptors, a process required for the release of newly synthesized virions. A balance of NA activity with sialic acid binding affinity of hemagglutinin (HA) is important for optimal virus replication. NA sequ...

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Veröffentlicht in:	PloS one 2013-08, Vol.8 (8), p.e71401-e71401
Hauptverfasser:	Marathe, Bindumadhav M, Lévêque, Vincent, Klumpp, Klaus, Webster, Robert G, Govorkova, Elena A
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Analysis Animals Avian flu Biological evolution Biology Chick Embryo Criteria Dogs Enzymatic activity Enzyme activity Enzyme Assays - standards Enzymes Exo-a-sialidase Fitness Fluorescence Fluorescent Dyes - chemistry Glycoproteins Hemagglutinins Humans Hymecromone - analogs & derivatives Hymecromone - chemistry Infectious diseases Influenza Influenza A Virus, H1N1 Subtype - enzymology Influenza viruses Interference Kinetics Laboratories Lectins Madin Darby Canine Kidney Cells Mass spectrometry Medicine N-Acetylneuraminic acid Neuraminidase - chemistry Organic acids Pandemics Parameter estimation Pathogenicity Pathogens Proteins Receptors Reproductive fitness Scientific imaging Signal-To-Noise Ratio Studies Substrates Surveillance Vaccines Viral Proteins - chemistry Virions Virology Viruses
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