Pathogen adhesins recognizing fucosylated host glycans

Pathogen adhesins recognizing fucosylated host glycans are microbial surface proteins that mediate the attachment of bacteria and viruses to host epithelial cells by binding to fucose-containing carbohydrate structures (Magalhães et al., 2015, PMID: 26433405). These glycans, including H-type antigens and Lewis antigens (e.g., Lewis b, Lewis x), are widely distributed in the mucus and on the cell surfaces of the gastrointestinal and respiratory tracts. Key examples include the BabA adhesin of Helicobacter pylori, which facilitates gastric colonization, and the LecB lectin of Pseudomonas aeruginosa, which is critical for biofilm architecture and lung infection (Titz, 2017, PMID: 28841286). Noroviruses also utilize these fucosylated histo-blood group antigens (HBGAs) as essential attachment factors for entry into intestinal cells (Ruvoën-Clouet et al., 2013, PMID: 23764352). Because these interactions are the first step in many infections, they are prime targets for anti-adhesion therapies. Such therapies employ glycomimetics or natural human milk oligosaccharides, like 2'-fucosyllactose, to act as decoys that competitively block the adhesin's binding site, thereby preventing pathogen colonization and reducing the risk of disease (Weichert et al., 2016, PMID: 27161353).

Other names

Fucose-binding lectinsFucose-specific microbial adhesinsHisto-blood group antigen (HBGA)-binding adhesinsFucose-recognizing binding proteins

Competitive inhibition of pathogen attachment to host cell surface glycans by acting as decoy ligands or high-affinity blockers of the adhesin binding site (Weichert et al., 2016, PMID: 27161353).