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Galactoside 2-alpha-L-fucosyltransferase 2 (FUT2) is a glycosyltransferase enzyme responsible for transferring fucose to galactose-containing glycans on glycoproteins and glycolipids, particularly on mucosal surfaces and bodily fluids. This reaction is essential for the biosynthesis of the H antigen, a precursor for ABO blood group antigens outside the red blood cell, a determinant of the "secretor" phenotype. Secretor status influences host–microbe interactions, susceptibility to a broad array of infections (notably norovirus and rotavirus), and modulates the composition of the gut and airway microbiota. Genetic variation in FUT2 underlies population-level differences in infection susceptibility and disease risk, including gastrointestinal illness, autoimmune diseases like Crohn's disease, and respiratory illnesses. Approximately 20% of many populations are non-secretors due to null mutations, resulting in absence of H antigens in secretions and differential susceptibility to pathogens that utilize blood group antigens for cell attachment. Non-secretors are largely resistant to certain norovirus strains but may have altered disease risk for other infections and chronic diseases. So far, there are no approved drugs that directly target FUT2; modulation of this enzyme or the pathway remains of significant research interest.
Inhibitors (hypothetical or experimental) would prevent the addition of fucose residues, blocking formation of H antigens and subsequent pathogen attachment
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