Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide

Marchetti, Roberta; Malinovská, Lenka; Lameignère, Emilie; Adamová, Lenka; Castro, Cristina De; Cioci, Gianluca; Stanetty, Christian; Kosma, Paul; Molinaro, Antonio; Wimmerová, Michaela; Imberty, Anne; Silipo, Alba

doi:10.1093/glycob/cws105

Cited by 29 publications

(32 citation statements)

References 35 publications

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“…This data also reinforces the conclusion made by Marchetti et al, that a lack of an STD effect of D-rhamnose (i.e., 6-deoxy D-mannose) with BC2L-A by NMR spectroscopy resulted from the loss in affinity of such 6-deoxygenated mannose-derivatives. 20 Variation of the aglycon in mannosides 12-15 had only a minor effect (7.0 -14.5 µM), and methyl glycoside α-12 was as potent as the bulky β-15 (IC50 = 7.0 µM for 12 and 7.4 µM for 15).…”

Section: Resultsmentioning

confidence: 99%

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Development of a competitive binding assay for the Burkholderia cenocepacia lectin BC2L-A and structure activity relationship of natural and synthetic inhibitors

et al. 2016

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Section: Resultsmentioning

confidence: 99%

“…Marchetti et al later showed, that BC2L-A binds also to L-glycero-D-manno-heptose which is a major constituent of bacterial lipopolysaccharide. 20 The stereochemistry of the glycol side chain was important for binding and methyl α-L,D-mannoheptoside bound with a Kd of 54 µM, while its C6 epimer did not bind.…”

Section: Introductionmentioning

confidence: 99%

Development of a competitive binding assay for the Burkholderia cenocepacia lectin BC2L-A and structure activity relationship of natural and synthetic inhibitors

et al. 2016

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“…It presents several opposing binding surfaces: The N-terminal domain trimers (two, facing top and bottom of the hexamer) are selective for fucosides; conversely, the C-terminal domain dimers (three, forming a central belt) specifically bind to mannosides [11]. BC2L-C C-terminal domain would allow binding of the lectin to the bacterial cell wall through recognition of manno-configured carbohydrates, as observed for its homolog BC2L-A, another soluble lectin from B. cenocepacia [32]. On the other hand, the N-terminal domain would target fucosylated ligands on host cells, in particular human blood group oligosaccharides.…”

Section: Discussionmentioning

confidence: 99%

BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information

2020

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Lectins mediate adhesion of pathogens to host tissues, filling in a key role in the first steps of infection. Belonging to the opportunistic pathogen Burkholderia cenocepacia, BC2L-C is a superlectin with dual carbohydrate specificity, believed to mediate cross-linking between bacteria and host cells. Its C-terminal domain binds to bacterial mannosides while its N-terminal domain (BCL2-CN) recognizes fucosylated human epitopes. BC2L-CN presents a tumor necrosis factor alpha (TNF-α) fold previously unseen in lectins with a novel fucose binding mode. We report, here, the production of a novel recombinant form of BC2L-CN (rBC2L-CN2), which allowed better protein stability and unprecedented co-crystallization with oligosaccharides. Isothermal calorimetry measurements showed no detrimental effect on ligand binding and data were obtained on the binding of Globo H hexasaccharide and l-galactose. Crystal structures of rBC2L-CN2 were solved in complex with two blood group antigens: H-type 1 and H-type 3 (Globo H) by X-ray crystallography. They provide new structural information on the binding site, of importance for the structural-based design of glycodrugs as new antimicrobials with antiadhesive properties.

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“…BclB and BclC have additional N-terminal domains. BclA forms homodimers with a strict specificity for oligomannose-type oligosaccharides, present on human glycoproteins 91 , 92 . BclC forms hexamers and has an N-terminal domain displaying a TNF-α-like fold with fucose-binding properties.…”

Section: The Role Of Qs In Biofilm Formation Of Members Of the Bccmentioning

confidence: 99%

Two quorum sensing systems control biofilm formation and virulence in members of theBurkholderia cepaciacomplex

et al. 2013

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The Burkholderia cepacia complex (Bcc) consists of 17 closely related species that are problematic opportunistic bacterial pathogens for cystic fibrosis patients and immunocompromised individuals. These bacteria are capable of utilizing two different chemical languages: N-acyl homoserine lactones (AHLs) and cis-2-unsaturated fatty acids. Here we summarize the current knowledge of the underlying molecular architectures of these communication systems, showing how they are interlinked and discussing how they regulate overlapping as well as specific sets of genes. A particular focus is laid on the role of these signaling systems in the formation of biofilms, which are believed to be highly important for chronic infections. We review genes that have been implicated in the sessile lifestyle of this group of bacteria. The new emerging role of the intracellular second messenger cyclic dimeric guanosine monophosphate (c-di-GMP) as a downstream regulator of the fatty acid signaling cascade and as a key factor in biofilm formation is also discussed.

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Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide

Cited by 29 publications

References 35 publications

Development of a competitive binding assay for the Burkholderia cenocepacia lectin BC2L-A and structure activity relationship of natural and synthetic inhibitors

Development of a competitive binding assay for the Burkholderia cenocepacia lectin BC2L-A and structure activity relationship of natural and synthetic inhibitors

BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information

Two quorum sensing systems control biofilm formation and virulence in members of theBurkholderia cepaciacomplex

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