LAMEIGNERE, Emilie, Lenka MALINOVSKÁ, Margita SLÁVIKOVÁ, Eric DUCHAUD, Edward P. MITCHELL, Annabelle VARROT, Ondrej ŠEDO, Anne IMBERTY and Michaela WIMMEROVÁ. Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. Biochemical Journal. 2008, vol. 411, No 2, p. 307-318. ISSN 0264-6021.
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Basic information
Original name Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia
Name in Czech Strukturní podstata rozpoznávaní mannosy lektinem z podmíněně patogenní bakterie Burkholderia cenocepacia
Authors LAMEIGNERE, Emilie (250 France), Lenka MALINOVSKÁ (203 Czech Republic, belonging to the institution), Margita SLÁVIKOVÁ (203 Czech Republic), Eric DUCHAUD (250 France), Edward P. MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Annabelle VARROT (250 France), Ondrej ŠEDO (203 Czech Republic, belonging to the institution), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution).
Edition Biochemical Journal, 2008, 0264-6021.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 4.371
RIV identification code RIV/00216224:14310/08:00024682
Organization unit Faculty of Science
UT WoS 000255384800011
Keywords in English bacterial lectin; Burkholderia cenocepacia; cepacia complex; mannose-binding lectin; Pseudomonas aeruginosa
Tags bacterial lectin, Burkholderia cenocepacia, cepacia complex, mannose-binding lectin, Pseudomonas aeruginosa
Tags International impact
Changed by Changed by: Mgr. Michal Petr, učo 65024. Changed: 9/12/2014 09:04.
Abstract
Chronic colonization of the lungs by opportunist bacteria such as Pseudomonas aeruginosa and members of the Bcc (Burkholderia cepacia complex) is the major cause of morbidity and mortality among CF (cystic fibrosis) patients. PA-IIL (lecB gene), a soluble lectin from Ps. aeruginosa, has been the subject of much interest because of its very strong affinity for fucose. Orthologues have been identified in the opportunist bacteria Ralstonia solanacearum, Chromobacterium violaceum and Burkholderia of Bcc. The genome of the J2315 strain of B. cenocepacia, responsible for epidemia in CF centres, contains three genes that code for proteins with PA-IIL domains. The shortest genewas cloned in Escherichia coli and pure recombinant protein, BclA (B. cenocepacia lectin A), was obtained. The presence of native BclA in B. cenocepacia extracts was checked using a proteomic approach. The specificity of recombinant BclA was characterized using surface plasmon resonance showing a preference for mannosides and supported with glycan array experiments demonstrating a strict specificity for oligomannose-type N-glycan structures.
Abstract (in Czech)
BclA lektin byl strukturně a termodynamicky charakterizován. Lektin vykazuje vysokou specifitu vůči mannosylovaným sacharidům.
Links
GA303/06/0570, research and development projectName: Strukturně-funkční studie lektinů a adhezinů patogenních mikroorganismů
Investor: Czech Science Foundation, Structure-function studies on lectins and adhesins from microbial patogens
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
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
MSM0021622415, plan (intention)Name: Molekulární podstata buněčných a tkáňových regulací
Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations
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