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

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

is not subject to a state or trade secret

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

Cite

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.

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