Sialidase activity in rimantadine-resistant and -sensitive influenza A viruses.
Rimantadine-resistant and -sensitive influenza A variants were assayed for their sialidase (neuraminidase, EC 3.2.1.18) activity. The kinetic parameters determined (pH optimum, stability against different pH values, thermal stability, activity on methylumbelliferyl-alpha-D-N-acetylneuraminic acid, N-acetylneuraminyl-lactose, fetuin and bovine submandibular gland mucin as substrates, Km with the former substrate, inhibition by two competitive inhibitors, and behavior towards amantadine) revealed the same results for both variants of the virus. Thus, it can be deduced that resistance to rimantadine does not influence the sialidase activity of influenza A virus.
Garcia-Sastre
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Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Salamanca, Spain.
Villar
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E
Hannoun
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Cabezas
J A
JA
D000818:Animals; D002642:Chick Embryo; D004352:Drug Resistance, Microbial / Q000502:physiology; D009980:Influenza A virus / Q000187:drug effects / Q000201:enzymology*; D007700:Kinetics; D009439:Neuraminidase / Q000378:metabolism*; D012299:Rimantadine / Q000494:pharmacology*; D013379:Substrate Specificity
D012299:Rimantadine; D009439:Neuraminidase