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Pathogen surface lectins are a diverse class of carbohydrate-binding proteins expressed on the exterior of viruses, bacteria, fungi, and parasites. These proteins are fundamental to the infectious process, as they mediate the specific recognition and attachment of pathogens to host cell-surface glycoconjugates, a prerequisite for colonization and invasion [4, 7, 10]. Beyond simple adhesion, pathogen lectins contribute to tissue tropism, the formation of protective biofilms, and the subversion of host immune responses [4, 12, 13]. Because these lectins are often essential for virulence but not for basic pathogen viability, they represent attractive targets for anti-adhesion therapies that aim to prevent or treat infections without driving the rapid development of antimicrobial resistance [1, 4, 12]. Therapeutic approaches currently under investigation include the use of small-molecule glycomimetics, multivalent carbohydrate scaffolds, and lectin-directed prodrugs designed to deliver antimicrobial payloads specifically to the site of infection [2, 6, 13]. Drugs such as Sibofimloc target specific bacterial lectins like FimH to treat conditions like Crohn's disease and urinary tract infections [3, 7]. However, challenges remain in achieving high binding affinity and avoiding cross-reactivity with endogenous host lectins [2, 17].
Inhibition of pathogen adhesion to host cells, disruption of biofilm architecture, and neutralization of viral entry by blocking carbohydrate-protein interactions.
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