The Dual Role of Bacterial Sialidases: Pathogenesis and Pharmacological Targeting
DOI:
https://doi.org/10.55640/Keywords:
Bacterial Sialidases, Neuraminidase, Sialic AcidAbstract
Sialic acids are a diverse family of nine-carbon acidic sugars that are typically found at the termini of glycoconjugates on eukaryotic cell surfaces and in secreted molecules [1, 2]. These ubiquitous sugars play crucial roles in numerous biological processes, including cell-cell recognition, immune responses, and host-pathogen interactions [1, 45]. Bacterial sialidases (also known as neuraminidases, EC 3.2.1.18) are enzymes that hydrolyze the glycosidic linkages of sialic acids, releasing free sialic acid [3, 7]. These enzymes are widely distributed among bacteria and exhibit diverse substrate specificities and biological functions [2, 7, 37]. Bacterial sialidases are involved in various aspects of bacterial physiology and pathogenesis, including nutrient acquisition, adhesion, immune evasion, and tissue invasion [6, 19, 24, 36]. Understanding the biological significance of bacterial sialidases is crucial for comprehending host-microbe interactions and developing strategies to combat bacterial infections. Furthermore, the unique properties of bacterial sialidases have led to their exploration for various biotechnological and therapeutic applications, such as in glycoconjugate engineering and as potential targets for antimicrobial therapies [7, 65]. This article reviews the biological roles of bacterial sialidases and discusses their current and potential applications.
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