Journal
PLOS PATHOGENS
Volume 7, Issue 9, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.ppat.1002238
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Funding
- French Ministry of Foreign and European Affairs
- Ministry of Education of the Czech Republic [MSM0021622413, LC6030, ME08008]
- Czech Science Foundation [GD301/09/H004GA, 303/09/1168]
- CEITEC - Central European Institute of Technology [CZ.1.05/1.1.00/02.0068]
- CNRS
- Vaincre la Mucoviscidose
- COST action [BM1003]
- European Community [205872]
- FWF [P19295, P 22909]
- Cystic Fibrosis Canada
- Canadian Institutes of Health Research
- Austrian Science Fund (FWF) [P 22909] Funding Source: researchfish
- Austrian Science Fund (FWF) [P19295] Funding Source: Austrian Science Fund (FWF)
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Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia, which has two distinct domains with unique specificities and biological activities. The N-terminal domain is a novel TNF-alpha-like fucose-binding lectin, while the C-terminal part is similar to a superfamily of calcium-dependent bacterial lectins. The C-terminal domain displays specificity for mannose and L-glycero-D-manno-heptose. BC2L-C is therefore a superlectin that binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes. The apo form of the C-terminal domain crystallized as a dimer, and calcium and mannose could be docked in the binding site. The whole lectin is hexameric and the overall structure, determined by electron microscopy and small angle X-ray scattering, reveals a flexible arrangement of three mannose/heptose-specific dimers flanked by two fucose-specific TNF-alpha-like trimers. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-alpha-like domain triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, and is therefore proposed to play a role in the dysregulated proinflammatory response observed in B. cenocepacia lung infections. The unique architecture of this newly recognized superlectin correlates with multiple functions including bacterial cell cross-linking, adhesion to human epithelia, and stimulation of inflammation.
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