Multispecific lectin that is able to recognize L-fucose in all possible linkages (PubMed:23695231). These could be found not only in decomposed plant matter in soil, which is the natural environment for A.fumigatus, but also in various epitopes on human tissues (By similarity). Mediates binding of A.fumigatus conidia to airway mucin in a fucose dependent manner (By similarity). Stimulates IL-8 production by human bronchial cells in a dose-dependent manner, contributing to the inflammatory response observed upon the exposure of a patient to A.fumigatus, and thus might be an important virulence factor involved in an early stage of A.fumigatus infection (By similarity). Homodimer (By similarity). AFL adopts the six-bladed beta-propeller fold and contains six binding sites per monomer, each located between two adjacent blades (By similarity). The six binding sites that are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition (By similarity). Lectins have particular value as specific probes for investigating the distribution, structure and biological function of carbohydrate chains on the cell surface of animal, plant, and microorganism because of their specificity for defined carbohydrate structures. AFL is suitable for detecting core fucose on cell surface glycoproteins. Belongs to the fungal fucose-specific lectin family.