Binding of different monosaccharides by lectin PA‐IIL from <i>Pseudomonas aeruginosa</i>: Thermodynamics data correlated with X‐ray structures

Sabin, C.; Mitchell, Edward P.; Pokorná, Martina; Gautier, Catherine; Utille, J.P.; Wimmerová, Michaela; Imberty, Anne

doi:10.1016/j.febslet.2006.01.030

Cited by 95 publications

(116 citation statements)

References 24 publications

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“…Binding data for PA-IIL interacting with different carbohydrates, glycomimetics, and glycopolymers. À7.5 1 [20] Me-a-Man 71 10 3 À5.7 0.04 [49] Me-a-Fuc 430 À8.7 6.7 [49] Lewis a 210 À9.1 13.8 [20] 20 310 À8.9 9.3 [19] [43] 36 80 20 [44] [a] Values from ITC and ELLA, respectively. …”

Section: Resultsmentioning

confidence: 99%

Glycomimetics and Glycodendrimers as High Affinity Microbial Anti‐adhesins

Imberty

Chabre

Roy

2008

Chemistry A European J

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237

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Adhesion to epithelial surface is often the first step in bacterial and viral infection. In this process, the microbes use a variety of proteins for interaction with host carbohydrates presented as glycoconjugates on cell surfaces. Crystal structures of adhesin and lectin binding sites in complexes with oligosaccharide open the route for design and synthesis of glycomimetics, glycodendrimers, and glycopolymers that are able to block infection at an early stage.

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Section: Resultsmentioning

confidence: 99%

Glycomimetics and Glycodendrimers as High Affinity Microbial Anti‐adhesins

Imberty

Chabre

Roy

2008

Chemistry A European J

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237

151

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“…9, 10 The architecture of the binding site leads to a special requirement for the hydroxyl stereochemistry of the interacting sugar that must be in either 1 C 4 -L-galacto or 4 C 1 -D-manno configuration, respectively. 11 The most potent monosaccharide ligands are methyl-a-L-fucoside and L-fucose with equilibrium dissociation constants of 0.43 lM and 2.9 lM, respectively. With respect to sugar stereochemistry, binding of methyl derivatives of D-arabinose, L-galactose ( 1 C 4 -L-galacto configuration), and D-mannose ( 4 C 1 -D-manno configuration), albeit with substantially lower affinities, has been proven by isothermal titration calorimetry (ITC).…”

Section: Introductionmentioning

confidence: 99%

Recognition of selected monosaccharides by Pseudomonas aeruginosa Lectin II analyzed by molecular dynamics and free energy calculations

Mishra

Křı́ž

Wimmerová

et al. 2010

Carbohydrate Research

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“…28,29,46,47 The tetrameric LecB has outstandingly high affinity to fucose and also binds mannose with an affinity comparable to ConA. 48 The homodimeric protein Bc2L-A exhibits strict specificity to mannose-terminating N-glycans.…”

Section: -26mentioning

confidence: 99%

Lectins from opportunistic bacteria interact with acquired variable-region glycans of surface immunoglobulin in follicular lymphoma

Schneider

Minden

Alkhatib

et al. 2015

Blood

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Key Points• BCR variable-region mannoses in follicular lymphoma are recognized by lectins of common opportunistic bacteria.• Introduction of N-linked sugars into the BCR variable region interferes with antigen recognition.B-cell antigen receptor (BCR) expression is a key feature of most B-cell lymphomas, but the mechanisms of BCR signal induction and the involvement of autoantigen recognition remain unclear. In follicular lymphoma (FL) B cells, BCR expression is retained despite a chromosomal translocation that links the antiapoptotic gene BCL2 to the regulatory elements of immunoglobulin genes, thereby disrupting 1 heavy-chain allele. A remarkable feature of FL-BCRs is the acquisition of potential N-glycosylation sites during somatic hypermutation. The introduced glycans carry mannose termini, which create potential novel binding sites for mannose-specific lectins. Here, we investigated the effect of N-linked variable-region glycosylation for BCR interaction with cognate antigen and with lectins of different origins. N-glycans were found to severely impair BCR specificity and affinity to the initial cognate antigen. In addition, we found that lectins from Pseudomonas aeruginosa and Burkholderia cenocepacia bind and stimulate FL cells. Human exposure to these bacteria can occur by contact with soil and water. In addition, they represent opportunistic pathogens in susceptible hosts. Understanding the role of bacterial lectins might elucidate the pathogenesis of FL and establish novel therapeutic approaches. (Blood. 2015;125(21):3287-3296)

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Binding of different monosaccharides by lectin PA‐IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X‐ray structures

Cited by 95 publications

References 24 publications

Glycomimetics and Glycodendrimers as High Affinity Microbial Anti‐adhesins

Glycomimetics and Glycodendrimers as High Affinity Microbial Anti‐adhesins

Recognition of selected monosaccharides by Pseudomonas aeruginosa Lectin II analyzed by molecular dynamics and free energy calculations

Lectins from opportunistic bacteria interact with acquired variable-region glycans of surface immunoglobulin in follicular lymphoma

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