Towards a Structural Basis for the Relationship Between Blood Group and the Severity of El Tor Cholera

Mandal, Pintu Kumar; Branson, Thomas R.; Hayes, Edward D.; Ross, James F.; Gavín, José A.; Daranas, Antonio Hernández; Turnbull, W. Bruce

doi:10.1002/ange.201109068

Cited by 3 publications

(3 citation statements)

References 32 publications

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“…Three structurally related toxins of the cholera toxin family: Vibrio cholerae Toxin Subunit B of the O1 classical biotype (Classical CTB, cCTB) and the El Tor biotype (El Tor CTB), and the enterotoxigenic Escherichia coli heat-labile Toxin (LTBh) 57 were investigated here. In contrast to the findings with BKPyV and JCPyV VP1s, the covalent and the noncovalent arrays exhibited robust binding (Fig 5D-F).…”

Section: Bacterial Toxinsmentioning

confidence: 99%

“…With the three types of FAA arrays binding of the three toxins could be detected to non-sialyl glycans [61][62][63][64] , Greater differences were observed in the different array formats that with the ganglioside related sequences. For example, binding to Le y probe (#13), the known ligand for the three toxins 57 , was well detected in the covalent CL array but only weakly in the HD arrays and almost absent in the noncovalent array. In contrast, the LacNAc-terminating glycans were more prominently bound in the noncovalent array compared to the covalent arrays: the complex type N-glycan (#36) was bound by all three toxins, and LNnT (#5) and LN3 (#6) by the cCTB and LTBh.…”

Section: Bacterial Toxinsmentioning

confidence: 99%

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Novel multifunctional glycan probes to elucidate specificities of diverse glycan recognition systems

Decout

Maio

et al. 2023

Preprint

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Glycan microarrays of sequence-defined glycans are the most widely used approach for high-throughput studies of interactions of glycans with glycan-binding proteins. Currently, nitrocellulose (NC) coated or N-hydroxysuccinimide (NHS) functionalized glass slides are the two most commonly used surfaces for immobilizing glycan probes as noncovalent and covalent arrays, respectively. The mode of glycan presentation can have an influence on the microarray readouts and is an important consideration in the glycan recognition knowledgebase. Here we present the development of glycan probes, tagged with a novel type of tri-functional Fmoc-amino-azido (FAA) linker, which can be readily converted into lipid-tagged or amino-terminating glycan probes for generating neoglycolipid (NGL)-based noncovalent arrays as well as covalent arrays. The azido functionality in the FAA glycan probes provides a means to light up the glycans via biorthogonal Click chemistry so that they become scanner-readable on the covalent arrays, which represents an advance in array quality control. Here analyses were carried out with a diverse set of 36 glycan-binding proteins (GBPs) to compare the performance of 44 glycans presented in a liposomal formulation as noncovalent arrays on NC-coated slides and on two types of NHS slides as covalent arrays. With most of the anti-glycan antibodies and plant lectins investigated, there were negligible or subtle differences in the binding detected in different arrays. However, there were some striking differences observed between the covalent and noncovalent arrays. These include the binding of Lotus Tetragonolobus Lectin (LTL) on the covalent but not the noncovalent arrays, and a clear preference observed for glycans on the noncovalent array in the binding of adhesins (VP1 proteins) of two human polyomaviruses JCPyV and BKPyV, and the human immune lectins Siglecs 7 and 9. Subtle yet significant differences in the binding to low-affinity glycan ligands were also observed with three bacterial toxins in different arrays. These results revealed interesting insights into the binding behaviour of different GBPs on the noncovalent and covalent arrays and highlight the importance to consider different array platforms in elucidating glycan-mediated interactions. The FAA glycan probes can be readily rendered fluorescent via Click chemistry in solution, enabling the detection of GBPs at the surface of cells.

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Section: Bacterial Toxinsmentioning

confidence: 99%

Section: Bacterial Toxinsmentioning

confidence: 99%

Novel multifunctional glycan probes to elucidate specificities of diverse glycan recognition systems

Decout

Maio

et al. 2023

Preprint

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“…87 Similarly, galactose and fucose copolymers were more effective inhibitors of CTx binding to human enteroids than galacto-or fuco-polymers alone, due to the additional lower-affinity fucosebinding site. 88,89 What is clear is that most materials strategies currently rely on trial and error to judge benefits (or not) from heterogeneity. The challenge of the polymer sequence for example, where extended sequences of one glycan may emerge, rather than a pure statistical distribution in a copolymer, makes quantification of the exact role of each component a major challenge.…”

Section: ■ 3d Presentationmentioning

confidence: 99%

Toward Glycomaterials with Selectivity as Well as Affinity

Richards

Gibson

2021

JACS Au

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Multivalent glycosylated materials (polymers, surfaces, and particles) often show high affinity toward carbohydrate binding proteins (e.g., lectins) due to the nonlinear enhancement from the cluster glycoside effect. This affinity gain has potential in applications from diagnostics, biosensors, and targeted delivery to anti-infectives and in an understanding of basic glycobiology. This perspective highlights the question of selectivity, which is less often addressed due to the reductionist nature of glycomaterials and the promiscuity of many lectins. The use of macromolecular features, including architecture, heterogeneous ligand display, and the installation of non-natural glycans, to address this challenge is discussed, and examples of selectivity gains are given.

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“Rules of Engagement” of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling

et al. 2016

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Understanding the dynamics of protein–ligand interactions, which lie at the heart of host–pathogen recognition, represents a crucial step to clarify the molecular determinants implicated in binding events, as well as to optimize the design of new molecules with therapeutic aims. Over the last decade, advances in complementary biophysical and spectroscopic methods permitted us to deeply dissect the fine structural details of biologically relevant molecular recognition processes with high resolution. This Review focuses on the development and use of modern nuclear magnetic resonance (NMR) techniques to dissect binding events. These spectroscopic methods, complementing X‐ray crystallography and molecular modeling methodologies, will be taken into account as indispensable tools to provide a complete picture of protein–glycoconjugate binding mechanisms related to biomedicine applications against infectious diseases.

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Towards a Structural Basis for the Relationship Between Blood Group and the Severity of El Tor Cholera

Cited by 3 publications

References 32 publications

Novel multifunctional glycan probes to elucidate specificities of diverse glycan recognition systems

Novel multifunctional glycan probes to elucidate specificities of diverse glycan recognition systems

Toward Glycomaterials with Selectivity as Well as Affinity

“Rules of Engagement” of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling

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