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The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications.

Supporting information

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Portable Document Format (PDF) file https://doi.org/10.1107/S1399004714026595/mh5137sup1.pdf
Supplementary Figures S1-S8 showing more details concerning the crystal structures of AFL complexes, SPR fitting data and saccharide structures used within the study.

PDB references: AFL, apo, 4uou; complex with Lewis Y trisaccharide, 4d4u; complex with BGA, 4ah4; complex with αFuc(1–6)GlcNAc, 4agt; complex with L-Gal, 4d52; complex with βMeFuc, 4c1y; complex with a mixture of fucosylated monosaccharides, 4aha


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