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@article{1300635,
author = {Houser, Josef and Komárek, Jan and Cioci, Gianluca and Varrot, Annabelle and Imberty, Anne and Wimmerová, Michaela},
article_location = {HOBOKEN},
article_number = {March},
doi = {http://dx.doi.org/10.1107/S1399004714026595},
keywords = {Aspergillus fumigatus; lectin; SPR; protein-saccharide complex; pathogen},
language = {eng},
issn = {1399-0047},
journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
title = {Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent},
url = {http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf},
volume = {71},
year = {2015}
}
TY - JOUR
ID - 1300635
AU - Houser, Josef - Komárek, Jan - Cioci, Gianluca - Varrot, Annabelle - Imberty, Anne - Wimmerová, Michaela
PY - 2015
TI - Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
JF - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
VL - 71
IS - March
SP - 442-453
EP - 442-453
PB - WILEY-BLACKWELL
SN - 13990047
KW - Aspergillus fumigatus
KW - lectin
KW - SPR
KW - protein-saccharide complex
KW - pathogen
UR - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf
L2 - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf
N2 - 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.
ER -
HOUSER, Josef, Jan KOMÁREK, Gianluca CIOCI, Annabelle VARROT, Anne IMBERTY and Michaela WIMMEROVÁ. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. \textit{ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}. HOBOKEN: WILEY-BLACKWELL, 2015, vol.~71, March, p.~442-453. ISSN~1399-0047. Available from: https://dx.doi.org/10.1107/S1399004714026595.
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