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@article{571971,
author = {Perret, Stephanie and Sabin, Charles and Dumon, Claire and Pokorná, Martina and Gautier, Catherine and Galanina, Oxana and Ilia, Shahov and Bovin, Nicolai and Nicaise, Magali and Desmadril, Michel and GilboaandGarber, Nechama and Wimmerová, Michaela and Mitchell, Edward P. and Imberty, Anne},
article_number = {2},
keywords = {lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure; milk oligosaccharides},
language = {eng},
issn = {0264-6021},
journal = {Biochemical Journal},
title = {Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,},
volume = {389},
year = {2005}
}
TY - JOUR
ID - 571971
AU - Perret, Stephanie - Sabin, Charles - Dumon, Claire - Pokorná, Martina - Gautier, Catherine - Galanina, Oxana - Ilia, Shahov - Bovin, Nicolai - Nicaise, Magali - Desmadril, Michel - Gilboa-Garber, Nechama - Wimmerová, Michaela - Mitchell, Edward P. - Imberty, Anne
PY - 2005
TI - Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,
JF - Biochemical Journal
VL - 389
IS - 2
SP - 325-332
EP - 325-332
SN - 02646021
KW - lectin
KW - Pseudomonas aeruginosa
KW - cystic fibrosis
KW - crystal structure
KW - milk oligosaccharides
N2 - One of the mechanisms contributing to breast-feeding protection of the newborn against enteric diseases is related to the ability of human milk oligosaccharides to prevent attachment of pathogenic bacteria to the duodenual epithelium. Indeed, a variety of fucosylated oligosaccharides, specific to human milk, form part of the innate immune system. In this study, we demonstrate the specific blocking of PA-IIL, a fucose-binding lectin of the human pathogen Pseudomonas aeruginosa by milk oligosaccharides. Two fucosylated epitopes, Lewis a and 3-fucosyllactose (Lewis x glucose analogue) bind to the lectin with dissociation constants of 2.2 10-7 M and 3.6 10-7 M, respectively. Thermodynamic studies indicate that these interactions are dominated by enthalpy. The entropy contribution is slightly favourable when binding to fucose and to the highest affinity ligand, Lewis a. The high resolution X-ray structures of two complexes of PA-IIL with milk oligosaccharides allow the precise determination of the conformation of a trisaccharide and a pentasaccharide. The different types of interaction between the oligosaccharides and the protein involve not only hydrogen bonding, but also calcium- and water-bridged contacts, allowing a rationalization of the thermodynamic data. This study provides important structural information about compounds that could be of general application in new therapeutic strategies against bacterial infections.
ER -
PERRET, Stephanie, Charles SABIN, Claire DUMON, Martina POKORNÁ, Catherine GAUTIER, Oxana GALANINA, Shahov ILIA, Nicolai BOVIN, Magali NICAISE, Michel DESMADRIL, Nechama GILBOA-GARBER, Michaela WIMMEROVÁ, Edward P. MITCHELL a Anne IMBERTY. Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,. \textit{Biochemical Journal}. 2005, roč.~389, č.~2, s.~325-332. ISSN~0264-6021.
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