Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia

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Authors

LAMEIGNERE Emilie MALINOVSKÁ Lenka SLÁVIKOVÁ Margita DUCHAUD Eric MITCHELL Edward P. VARROT Annabelle ŠEDO Ondrej IMBERTY Anne WIMMEROVÁ Michaela

Year of publication 2008
Type Article in Periodical
Magazine / Source Biochemical Journal
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords bacterial lectin; Burkholderia cenocepacia; cepacia complex; mannose-binding lectin; Pseudomonas aeruginosa
Description 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.
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