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.

Central European Institute of Technology Masaryk University Kamenice 5 62500 Brno Czech Republic

CERMAV CNRS UPR5301 affiliated with Université de Grenoble and ICMG BP53 38041 Grenoble CEDEX 9 France

Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés Institut National des Sciences Appliquées 31077 Toulouse CEDEX France

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