Article Dans Une Revue Acta crystallographica Section D : Structural biology [1993-...] Année : 2015

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

Résumé

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.

Fichier principal
Vignette du fichier
AFL_HAL.pdf (1.48 Mo) Télécharger le fichier
Origine Fichiers produits par l'(les) auteur(s)
Licence

Dates et versions

hal-03641311 , version 1 (20-04-2022)

Licence

Identifiants

Citer

Josef Houser, Jan Komarek, Gianluca Cioci, Annabelle Varrot, Anne Imberty, et al.. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (3), pp.442-453. ⟨10.1107/S1399004714026595⟩. ⟨hal-03641311⟩
67 Consultations
225 Téléchargements

Altmetric

Partager

  • More