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Bacterial lectins are carbohydrate-binding proteins produced by bacteria that specifically recognize and bind certain sugar structures, typically on host cell surfaces or in the extracellular environment[2]. Their primary biological function is to mediate the attachment or adherence of bacteria to host cells, which is generally a prerequisite for bacterial colonization and subsequent infection[3]. In addition to mediating host interactions, some specialized bacterial lectins, such as lectin-like bacteriotoxic proteins, act as bacteriocins—they selectively kill related bacterial species through mechanisms involving specific carbohydrate recognition domains[1]. Structurally, many bacterial lectins resemble plant lectins and may possess multiple carbohydrate-binding domains with specificity for sugars like mannose[1]. While bacterial lectins are considered therapeutic targets, especially in the context of blocking adhesion as an anti-infective strategy, there are challenges in developing drugs due to potential effects on commensal flora and host carbohydrate-binding proteins.
Drugs or inhibitors (glycomimetics) block lectin-carbohydrate binding, thereby preventing bacterial adhesion or colonization or antagonizing bacteriotoxic effects
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