Lectin-Based Method for Evaluation of Neuraminidase Activity and Its Inhibitors
Zuzana Hľasová 1
Stanislav Miertuš 1,2
Miroslav Ondrejovič 1
Jaroslav Katrlík 3
1 University of Ss. Cyril and Methodius in Trnava, Faculty of Natural Sciences, Department of Biotechnology, Nám. J. Herdu 2, 917 01 Trnava, Slovak Republic 2 International Centre for Applied Research and Sustainable Technology, Jamnického 19, 841 04 Bratislava, Slovak Republic 3 Slovak Academy of Sciences, Institute of Chemistry, Department of Glycobiotechnology, Dúbravská cesta 9, 845 38, Bratislava, Slovak Republic
|Section:||Organic, bioorganic and pharmaceutical chemistry, pharmacology|
Neuraminidases are hydrolytic enzymes acting on glycosidic linkage of terminal sialic acids in glycoproteins, glycolipids, oligosaccharides, colominic acids and synthetic substrates . Function of these enzymes is essential in pathogenesis of many viral and bacterial infections . Discovery of potent neuraminidase inhibitors, as well as development of high-throughput methods for their activity evaluation is therefore desirable in treatment and prophylaxis of these diseases [3 - 4]. In our work, we have developed a method for evaluation of neuraminidase activity and its inhibitors. In the developed lectin-based method, the lectin Peanut agglutinin (PNA) was used for the determination of galactose moiety exposed after cleavage of sialic acid from immobilized fetuin by neuraminidase from Clostridium perfringens. Described method was performed in microtiter-plates with quantification of desialylation by fluorescent dye. Our next aim is miniaturization of this method to microarray format.
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