Structural basis for the interaction between human milk
oligosaccharides and a bacterial protein, Pseudomonas
aeruginosa lectin PA-IIL,

J 2005

Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,

PERRET, Stephanie; Charles SABIN; Claire DUMON; Martina POKORNÁ; Catherine GAUTIER et. al.

Základní údaje

Originální název

Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,

Název česky

Strukturni zaklad interakci mezi proteinem PA-IIL z Pseudomona aeruginosa a mlecnymi oligosacharidy

Autoři

Vydání

Biochemical Journal, 2005, 0264-6021

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 4.224

Kód RIV

RIV/00216224:14310/05:00013769

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000230779000009

Klíčová slova anglicky

lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure; milk oligosaccharides

Štítky

Crystal Structure, cystic fibrosis, lectin, milk oligosaccharides, Pseudomonas aeruginosa

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 1. 2007 15:32, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

ORIG CZ

V originále

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.

Česky

Strukturni zaklad interakci mezi proteinem PA-IIL z Pseudomona aeruginosa a mlecnymi oligosacharidy

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

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,. Biochemical Journal. 2005, roč. 389, č. 2, s. 325-332. ISSN 0264-6021.

@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.

Přehled o publikaci