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Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.

Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.

Authors :
Houser J
Komarek J
Cioci G
Varrot A
Imberty A
Wimmerova M
Source :
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2015 Mar; Vol. 71 (Pt 3), pp. 442-53. Date of Electronic Publication: 2015 Feb 26.
Publication Year :
2015

Abstract

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.

Details

Language :
English
ISSN :
1399-0047
Volume :
71
Issue :
Pt 3
Database :
MEDLINE
Journal :
Acta crystallographica. Section D, Biological crystallography
Publication Type :
Academic Journal
Accession number :
25760594
Full Text :
https://doi.org/10.1107/S1399004714026595