Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
| Authors | |
|---|---|
| Year of publication | 2015 |
| Type | Article in Periodical |
| Magazine / Source | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY |
| MU Faculty or unit | |
| Citation | |
| Web | http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf |
| Doi | http://dx.doi.org/10.1107/S1399004714026595 |
| Field | Biochemistry |
| Keywords | Aspergillus fumigatus; lectin; SPR; protein-saccharide complex; pathogen |
| Description | 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. |
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