Kinetic studies on the sialidase of three influenza B and three influenza A virus strains.
Sialidase of influenza virus type A has been extensively studied through structural and kinetic approaches. However, sialidase of influenza virus type B has been less investigated. In this work, we have studied the activity and some properties (optimal pH, KM, Vmax, thermal stability) of sialidase in three influenza virus strains of type B (circulating in the period 1983-86) and also the activity and properties of sialidase from three virus strains of type A circulating at the same period of time. The results show that the activity and the Vmax was always higher for sialidase of type A viruses relative to those values of type B. Differences were also found for optimal pH and, in some cases, for thermal stability of the sialidase between strains belonging to the influenza viruses type A and B. However, the behaviour for the sialidase in all strains was very similar towards two competitive inhibitors. Thus, it could be suggested that the evolution pattern of the sialidase of both types of influenza viruses determines some modifications which result in a higher efficiency for sialidase of some strains of influenza virus type A, but maintaining in the two types of viruses a similar behaviour towards competitive inhibitors.
Cabezas
J A
JA
Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Salamanca, Spain.
Milicua
M
M
Bernal
C S
CS
Villar
E
E
Perez
N
N
Hannoun
C
C
D000818:Animals; D002645:Chickens; D004795:Enzyme Stability; D006384:Hemagglutination; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus / Q000201:enzymology*; D009981:Influenza B virus / Q000201:enzymology*; D007700:Kinetics; D009439:Neuraminidase / Q000378:metabolism*; D013379:Substrate Specificity
D009439:Neuraminidase