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.

Basic information

Original name

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

Name in Czech

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

Authors

PERRET, Stephanie (250 France), Charles SABIN (250 France), Claire DUMON (250 France), Martina POKORNÁ (203 Czech Republic), Catherine GAUTIER (250 France), Oxana GALANINA (643 Russian Federation), Shahov ILIA (643 Russian Federation), Nicolai BOVIN (643 Russian Federation), Magali NICAISE (643 Russian Federation), Michel DESMADRIL (250 France), Nechama GILBOA-GARBER (376 Israel), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Edward P. MITCHELL (826 United Kingdom of Great Britain and Northern Ireland) and Anne IMBERTY (250 France)

Edition

Biochemical Journal, 2005, 0264-6021

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 4.224

RIV identification code

RIV/00216224:14310/05:00013769

Organization unit

Faculty of Science

UT WoS

000230779000009

Keywords in English

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

Abstract

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.

In Czech

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

Links

LN00A016, research and development project

Name: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

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 and Anne IMBERTY. Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,. Biochemical Journal. 2005, vol. 389, No 2, p. 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 and Anne IMBERTY. Structural basis for the interaction between human milk oligosaccharides and a bacterial protein, Pseudomonas aeruginosa lectin PA-IIL,. \textit{Biochemical Journal}. 2005, vol.~389, No~2, p.~325-332. ISSN~0264-6021.

Detailed Information on Publication Record