Structural basis for oligosaccharide-mediated adhesion of
Pseudomonas aeruginosa in the lungs of cystic fibrosis patients

J 2002

Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients

MITCHELL, Edward, Corinne HOULES, Dvora SUDAKEVITZ, Michaela WIMMEROVÁ, Catherine GAUTIER et. al.

Basic information

Original name

Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients

Authors

MITCHELL, Edward (250 France), Corinne HOULES (250 France), Dvora SUDAKEVITZ (376 Israel), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Catherine GAUTIER (250 France), Serge PÉREZ (250 France), Albert M. WU (158 Taiwan), Nechama GILBOA-GARBER (376 Israel) and Anne IMBERTY (250 France)

Edition

Nature Structural Biology, New York, Nature America Inc. 2002, 1072-8368

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: 10.244

RIV identification code

RIV/00216224:14310/02:00007079

Organization unit

Faculty of Science

Keywords in English

lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure

Abstract

V originále

Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.

Links

LN00A016, research and development project

Name: BIOMOLEKULÁRNÍ CENTRUM

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

Citovat

MITCHELL, Edward, Corinne HOULES, Dvora SUDAKEVITZ, Michaela WIMMEROVÁ, Catherine GAUTIER, Serge PÉREZ, Albert M. WU, Nechama GILBOA-GARBER and Anne IMBERTY. Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients. Nature Structural Biology. New York: Nature America Inc., 2002, vol. 9, No 12, p. 918-921. ISSN 1072-8368.

@article{407796,
   author = {Mitchell, Edward and Houles, Corinne and Sudakevitz, Dvora and Wimmerová, Michaela and Gautier, Catherine and Pérez, Serge and Wu, Albert M. and GilboaandGarber, Nechama and Imberty, Anne},
   article_location = {New York},
   article_number = {12},
   keywords = {lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure},
   language = {eng},
   issn = {1072-8368},
   journal = {Nature Structural Biology},
   title = {Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients},
   volume = {9},
   year = {2002}
}

TY  - JOUR
ID  - 407796
AU  - Mitchell, Edward - Houles, Corinne - Sudakevitz, Dvora - Wimmerová, Michaela - Gautier, Catherine - Pérez, Serge - Wu, Albert M. - Gilboa-Garber, Nechama - Imberty, Anne
PY  - 2002
TI  - Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients
JF  - Nature Structural Biology
VL  - 9
IS  - 12
SP  - 918
EP  - 918
PB  - Nature America Inc.
SN  - 10728368
KW  - lectin
KW  - Pseudomonas aeruginosa
KW  - cystic fibrosis
KW  - crystal structure
N2  - Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.
ER  -

MITCHELL, Edward, Corinne HOULES, Dvora SUDAKEVITZ, Michaela WIMMEROVÁ, Catherine GAUTIER, Serge PÉREZ, Albert M. WU, Nechama GILBOA-GARBER and Anne IMBERTY. Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients. \textit{Nature Structural Biology}. New York: Nature America Inc., 2002, vol.~9, No~12, p.~918-921. ISSN~1072-8368.

Detailed Information on Publication Record