Interaction of Viruses, Bacteria and Bacterial Toxins with Host Cell Surface Glycolipids. Aspects on Receptor Identification and Dissection of Binding Epitopes

Bock, Klaus; Karlsson, Karl‐Anders; Strömberg, Nicklas; Teneberg, Susann

doi:10.1007/978-1-4613-1663-3_7

Cited by 23 publications

(14 citation statements)

References 52 publications

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“…Receptors for bacterial toxins. [127,129,212,213] Bacterium Toxin Ligand [a] Vibrio cholerae cholera toxin [214] S: GM 1 : Gal(b1,3)GalNAc(b1,4)(NeuAc(a2,3))Gal(b1,4)Glc(b)-ceramide [215,216] S: isoligands: [216] E. coli heat-labile toxin [217] S: GM1 [145] Clostridium tetani tetanus toxin S: Gal(b1,3)GalNAc(b1,4)((NeuAc(a2,8))NeuAc(2,3)Gal(b1,4)Glc(b)-ceramide [218] S: isoligands: NeuAc(a2 Clostridium botulinum botulinum toxin B [220] S: Gal(b)-ceramide…”

Section: Cellmentioning

confidence: 99%

Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors

Mammen

Choi

Whitesides

1998

Angewandte Chemie International Edition

3,782

1,662

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Found throughout biology, polyvalent interactions are characterized by the simultaneous binding of multiple ligands on one biological entity to multiple receptors on another (top part of the illustration) and have a number of characteristics that monovalent interactions do not (bottom). In particular, polyvalent interactions can be collectively much stronger than corresponding monovalent interactions, and they can provide the basis for mechanisms of both agonizing and antagonizing biological interactions that are fundamentally different from those available in monovalent systems.

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Section: Cellmentioning

confidence: 99%

Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors

Mammen

Choi

Whitesides

1998

Angewandte Chemie International Edition

3,782

1,662

View full text Add to dashboard Cite

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“…Since host carbohydrates have been known for many years to constitute specific attachment sites for pathogen protein receptors (6,7), there is great interest in structure-function studies of bacterial proteins enabling the pathogen attachment to host glycans. However, only a limited number of their complexes with receptors have been characterized by crystallography.…”

mentioning

confidence: 99%

The Fucose-binding Lectin from Ralstonia solanacearum

Kostlánová

Mitchell

Lortat‐Jacob

et al. 2005

Journal of Biological Chemistry

167

140

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Plant pathogens, like animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment, and invasion. The bacterium Ralstonia solanacearum, which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, R. solanacearum lectin, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to ␣Fuc1-2Gal and ␣Fuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for ␣Fuc1-2Gal-containing oligosaccharides (K D ‫؍‬ 2.5 ؋ 10 ؊7 M for 2-fucosyllactose). R. solanacearum lectin has been crystallized with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with ␣-methyl-fucoside being at ultrahigh resolution, reveal that each monomer consists of two small four-stranded anti-parallel ␤-sheets. Trimerization through a 3-fold or pseudo-3-fold axis generates a six-bladed ␤-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a ␤-propeller formed by oligomerization and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the ␤-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharide from the primary cell wall of plants, which may be the biological target of the lectin.

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“…In vivo, the blood flow generates mechanical forces that limit the binding of bacteria to the endothelium surface. [133][134][135] 132 Experimental studies using a flow chamber assay indicated that after their initial attachment to the surface of endothelial cells, the bacteria could resist high-velocity blood flow conditions.…”

Section: N Meningitidismentioning

confidence: 99%