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.
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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
Original 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
Tags Crystal Structure, cystic fibrosis, lectin, Pseudomonas aeruginosa
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Michaela Wimmerová, Ph.D., učo 854. Changed: 4/1/2007 15:29.
Abstract
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 projectName: BIOMOLEKULÁRNÍ CENTRUM
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center
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