Identification and characterization of a novel, versatile sialidase from a Sphingobacterium that can hydrolyze the glycosides of any sialic acid species at neutral pH.

Autor: Iwaki Y; Bioscience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan; Program for Leading Graduate Schools, Integrative Graduate Education and Research Program in Green Natural Sciences, Nagoya University, Nagoya, 464-8601, Japan., Matsunaga E; Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan., Takegawa K; Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan., Sato C; Bioscience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan; Program for Leading Graduate Schools, Integrative Graduate Education and Research Program in Green Natural Sciences, Nagoya University, Nagoya, 464-8601, Japan., Kitajima K; Bioscience and Biotechnology Center, Nagoya University, Nagoya, 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan; Program for Leading Graduate Schools, Integrative Graduate Education and Research Program in Green Natural Sciences, Nagoya University, Nagoya, 464-8601, Japan. Electronic address: kitajima@agr.nagoya-u.ac.jp.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2020 Mar 05; Vol. 523 (2), pp. 487-492. Date of Electronic Publication: 2019 Dec 27.
DOI: 10.1016/j.bbrc.2019.12.079
Abstrakt: Bacterial sialidases are widely used to remove sialic acid (Sia) residues from glycans. Most of them cleave the glycosides of N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) under acidic pHs; however, currently available bacterial sialidases had no activity to the glycosides of deaminoneuraminic acid (Kdn). In this study, we found a novel sialidase from Sphingobacterium sp. strain HMA12 that could cleave any of the glycosides of Neu5Ac, Neu5Gc, and Kdn. It also had a broad linkage specificity, i.e., α2,3-, α2,6-, α2,8-, and α2,9-linkages, and the optimal pH at neutral ranges, pH 6.5-7.0. These properties are particularly important when sialidases are applied for in vivo digestion of the cell surface sialosides under physiological conditions. Interestingly, 2,3-didehydro-2-deoxy-N-acetylneuraminic acid (Neu5Ac2en), which is a transition state analog-based inhibitor, competitively inhibited the enzyme-catalyzed reaction for Kdn as well as for Neu5Ac, suggesting that the active site is common to the Neu5Ac and Kdn residues. Taken together, this sialidase is versatile and useful for the in vivo research on sialo-glycoconjugates.
Competing Interests: Declaration of competing interest On behalf of all the authors for this manuscript, the corresponding author declare: None declared.
(Copyright © 2019 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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