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@article{763057,
author = {Lameignere, Emilie and Malinovská, Lenka and Sláviková, Margita and Duchaud, Eric and Mitchell, Edward P. and Varrot, Annabelle and Šedo, Ondrej and Imberty, Anne and Wimmerová, Michaela},
article_number = {2},
keywords = {bacterial lectin; Burkholderia cenocepacia; cepacia complex; mannose-binding lectin; Pseudomonas aeruginosa},
language = {eng},
issn = {0264-6021},
journal = {Biochemical Journal},
title = {Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia},
volume = {411},
year = {2008}
}
TY - JOUR
ID - 763057
AU - Lameignere, Emilie - Malinovská, Lenka - Sláviková, Margita - Duchaud, Eric - Mitchell, Edward P. - Varrot, Annabelle - Šedo, Ondrej - Imberty, Anne - Wimmerová, Michaela
PY - 2008
TI - Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia
JF - Biochemical Journal
VL - 411
IS - 2
SP - 307-318
EP - 307-318
SN - 02646021
KW - bacterial lectin
KW - Burkholderia cenocepacia
KW - cepacia complex
KW - mannose-binding lectin
KW - Pseudomonas aeruginosa
N2 - 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.
ER -
LAMEIGNERE, Emilie, Lenka MALINOVSKÁ, Margita SLÁVIKOVÁ, Eric DUCHAUD, Edward P. MITCHELL, Annabelle VARROT, Ondrej ŠEDO, Anne IMBERTY a Michaela WIMMEROVÁ. Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. \textit{Biochemical Journal}. roč.~411, č.~2, s.~307-318. ISSN~0264-6021. 2008.
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