Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25760594
DOI
10.1107/s1399004714026595
PII: S1399004714026595
Knihovny.cz E-resources
- Keywords
- Aspergillus fumigatus, SPR, lectin, pathogen, protein–saccharide complex,
- MeSH
- Aspergillus fumigatus chemistry MeSH
- Epithelium MeSH
- Fungal Proteins chemistry MeSH
- Lectins chemistry MeSH
- Humans MeSH
- Oligosaccharides chemistry MeSH
- Protein Structure, Tertiary MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fungal Proteins MeSH
- Lectins MeSH
- Oligosaccharides MeSH
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.
References provided by Crossref.org
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