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Updated: Sep 20, 2026

A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
Published on: May 29, 2016
Characterization of sialidase from an influenza A (H3N2) virus strain: kinetic parameters and substrate specificity
José França de Barros1, Daniela Sales Alviano, Maria Helena da Silva
1Departamento de Virologia, Instituto de Microbiologia Prof Paulo de Góes (IMPPG), Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Abstract:
Neuraminidase (NA) of influenza A (H3N2) viruses was characterized after purification by gel filtration and proteolytic treatment, using the X-31 variant strain that is a reassortment between the influenza A/Victoria/3/75 (responsible for the 1975 pandemic) and the influenza A/PR/8/34 virus samples, as a model. In the purification process, NA heads, that is the spike responsible for the virus sialidase activity, were purified by filtration through a Bio-Gel polyacrylamide column. The enzyme activity was determined by periodic acid/thiobarbituric acid assay and high-performance thin-layer chromatography. The sialidase showed preference for the alpha-2,3-linkage over the alpha-2,6-linkage of sialyllactoses (K(m) of 1.8 and 5.2 x 10(-4)M, respectively) at pH 5.2. The enzyme acted on natural and synthetic substrates at different hydrolysis rates, as well as on human erythrocytes (A group, Rh+) and yeast (CANDIDA ALBICANS) cells. The active NA produced by gel filtration was characterized by different parameters of its sialidase activity, also showing to be a suitable tool for the identification of natural sialocompounds and for the screening of antisialidase drugs to treat influenza virus infections.
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