ArticleThe Journal of biological chemistry2012
Fucose-binding lectin from opportunistic pathogen Burkholderia ambifaria binds to both plant and human oligosaccharidic epitopes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.
- Tandem-repeat lectins: structural and functional insights.Glycobiology · 2024Pooled it
- GlyContact analyzes glycan 3D structures at scale.Nature communications · 2025Article
- N‑Terminal Protein Complexation and Assembly with a Triangular Sulfated Macrocycle.Crystal growth & design · 2025Article
- Lectins and polysaccharide EPS I have flow-responsive roles in the attachment and biofilm mechanics of plant pathogenic Ralstonia.PLoS pathogens · 2024Article
- Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Quantitative analysis of fucosylated glycoproteins by immobilized lectin-affinity fluorescent labeling.RSC advances · 2023Article
- Fragment-Based Lead Discovery Strategies in Antimicrobial Drug Discovery.Antibiotics (Basel, Switzerland) · 2023Review
- Multivalent Fucosides Targeting β-Propeller Lectins from Lung Pathogens with Promising Anti-Adhesive Properties.ACS chemical biology · 2022Article
- Multivalent glycocyclopeptides: conjugation methods and biological applications.Chemical Society reviews · 2022Review
- Prevaccination Glycan Markers of Response to an Influenza Vaccine Implicate the Complement Pathway.Journal of proteome research · 2022Article
- Targeting undruggable carbohydrate recognition sites through focused fragment library design.Communications chemistry · 2022Article
- Druggable Allosteric Sites in β-Propeller Lectins.Angewandte Chemie (International ed. in English) · 2022Article
- Bacterial lectin BambL acts as a B cell superantigen.Cellular and molecular life sciences : CMLS · 2021Article
- Biochemical and structural studies of target lectin SapL1 from the emerging opportunistic microfungus Scedosporium apiospermum.Scientific reports · 2021Article
- Automated Glycan Assembly ofAngewandte Chemie (International ed. in English) · 2021Article
- Grafting Dendrons onto Pillar[5]Arene Scaffolds.Molecules (Basel, Switzerland) · 2021Review
- Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands forChemical science · 2020Article
- 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
- Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family.Molecules (Basel, Switzerland) · 2019Article
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Authors and funding
11 authors at 6 institutions in 5 countries.
Funding
Abstract
Burkholderia ambifaria is generally associated with the rhizosphere of plants where it has biocontrol effects on other microorganisms. It is also a member of the Burkholderia cepacia complex, a group of closely related bacteria that cause lung infections in immunocompromised patients as well as in patients with granulomatous disease or cystic fibrosis. Our previous work indicated that fucose on human epithelia is a frequent target for lectins and adhesins of lung pathogens (Sulák, O., Cioci, G., Lameignère, E., Balloy, V., Round, A., Gutsche, I., Malinovská, L., Chignard, M., Kosma, P., Aubert, D. F., Marolda, C. L., Valvano, M. A., Wimmerová, M., and Imberty, A. (2011) PLoS Pathog. 7, e1002238). Analysis of the B. ambifaria genome identified BambL as a putative fucose-binding lectin. The 87-amino acid protein was produced recombinantly and demonstrated to bind to fucosylated oligosaccharides with a preference for αFuc1-2Gal epitopes. Crystal structures revealed that it associates as a trimer with two fucose-binding sites per monomer. The overall fold is a six-bladed β-propeller formed by oligomerization as in the Ralstonia solanacearum lectin and not by sequential domains like the fungal fucose lectin from Aleuria aurantia. The affinity of BambL for small fucosylated glycans is very high as demonstrated by microcalorimetry (K(D) < 1 μM). Plant cell wall oligosaccharides and human histo-blood group oligosaccharides H-type 2 and Lewis Y are bound with equivalent efficiency. Binding to artificial glycosphingolipid-containing vesicles, human saliva, and lung tissues confirmed that BambL could recognize a wide spectrum of fucosylated epitopes, albeit with a lower affinity for biological material from nonsecretor individuals.
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