ArticlePLoS pathogens2011
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 69 citations in OpenAlex.
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- Toward Dual-Target Glycomimetics against Two Bacterial Lectins to FightJournal of medicinal chemistry · 2025Article
- The potential of the South African plant Tulbaghia Violacea Harv for the treatment of triple negative breast cancer.Scientific reports · 2025Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Identification of New L-Fucosyl and L-Galactosyl Amides as Glycomimetic Ligands of TNF Lectin Domain of BC2L-C fromMolecules (Basel, Switzerland) · 2023Article
- Glycomimetic antagonists of BC2L-C lectin: insights from molecular dynamics simulations.Frontiers in molecular biosciences · 2023Article
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- Targeting a Multidrug-Resistant Pathogen: First Generation Antagonists ofACS chemical biology · 2022Article
- Prediction and Validation of a Druggable Site on Virulence Factor of Drug Resistant Burkholderia cenocepacia*.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Development of 48-condition buffer screen for protein stability assessment.European biophysics journal : EBJ · 2021Article
- Glycan Array Technology.Advances in biochemical engineering/biotechnology · 2021Article
- One gene, multiple ecological strategies: A biofilm regulator is a capacitor for sustainable diversity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information.Molecules (Basel, Switzerland) · 2020Article
- Straight Forward and Versatile Differentiation of the l-Frontiers in chemistry · 2020Article
- Intracellular Burkholderia Symbionts induce extracellular secondary infections; driving diverse host outcomes that vary by genotype and environment.The ISME journal · 2019Article
- Investigation of the Binding Affinity of a Broad Array of l-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin.Molecules (Basel, Switzerland) · 2019Article
- Microbe-focused glycan array screening platform.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Microscopy examination of red blood and yeast cell agglutination induced by bacterial lectins.PloS one · 2019Article
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Authors and funding
14 authors at 9 institutions in 5 countries.
Funding
Abstract
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-α-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-α-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-α-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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.