Pathogen adhesion lectins

Pathogen adhesion lectins and adhesins are specialized proteins expressed on the surface of bacteria, viruses, fungi, and parasites that facilitate the initial step of infection by binding to specific glycan motifs on host cell surfaces (Varki et al., 2017). This interaction is crucial for pathogen colonization, tissue tropism, and the formation of biofilms, effectively anchoring the microbe to the host epithelium to resist mechanical clearance (Ofek et al., 2003). Because these interactions are often highly specific to the pathogen and the host tissue, they represent attractive targets for anti-adhesion therapies. Unlike traditional antibiotics that kill or inhibit the growth of microbes, drugs targeting these lectins—such as glycomimetics or small-molecule inhibitors—prevent the initial attachment. This approach reduces the selective pressure for resistance and spares the host's beneficial microbiota (Sharon, 2006). Current therapeutic strategies focus on developing high-affinity monovalent or multivalent carbohydrate analogs that competitively block the pathogen's binding sites. For example, FimH inhibitors like sibofimloc are being developed to treat urinary tract infections and Crohn's disease by preventing E. coli from adhering to the intestinal or bladder wall (Enterome, 2020). These targets are particularly valuable in the context of rising antimicrobial resistance, offering a non-bactericidal alternative to infection management.

Other names

Microbial lectinsPathogen adhesinsGlycan-binding proteinsHemagglutininsBacterial fimbriae proteinsPili adhesinsMicrobial glycan-binding adhesins

Competitive inhibition of pathogen-host glycan binding (Anti-adhesion therapy)