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Drickamer, Kurt; Taylor, Maureen E.

doi:10.1186/gb-2002-3-12-reviews1034

Cited by 68 publications

(24 citation statements)

References 7 publications

(10 reference statements)

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“…Even though the possible number of glycans found in the human body is estimated be quite large (100,000-500,000) due to variations that occur on their termini, smaller glycan arrays may capture much of the information encoded in the human glycome 30 . Glycan screening is particularly powerful in that it allows one to not only identify which glycans are bound by a particular lectin, but also which glycans are not bound 31 . Since the array contains entire glycans along with fragments of these often branched molecules, the specific carbohydrate footprint of the lectin on the larger glycans can be identified.…”

Section: Resultsmentioning

confidence: 99%

Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family

Kaus

Lary

Cole

et al. 2014

Journal of Molecular Biology

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Pore-forming toxins (PFTs) are a class of pathogen-secreted molecules that oligomerize to form transmembrane channels in cellular membranes. Determining the mechanism for how PFTs bind membranes is key to understanding their role in disease and possible ways to block their action. Vibrio vulnificus, an aquatic pathogen responsible for severe food poisoning and septicemia in humans, secretes a PFT called Vibrio vulnificus hemolysin (VVH), which contains a single C-terminal targeting domain predicted to resemble a β-trefoil lectin fold. In order to understand the selectivity of the lectin for glycan motifs, we expressed the isolated VVH β-trefoil domain and used glycan-chip screening to identify that VVH displays a preference for terminal galactosyl groups including N-acetyl-D-galactosamine (GalNAc) and N-acetyl-D-lactosamine (LacNAc). The X-ray crystal structure of the VVH lectin domain solved to 2.0 Å resolution reveals a heptameric ring arrangement similar to the oligomeric form of the related, but inactive, lectin from Vibrio cholerae cytolysin. Structures bound to glycerol, GalNAc, and LacNAc outline a common and versatile mode of recognition allowing VVH to target a wide variety of cell-surface ligands. Sequence analysis in light of our structural and functional data suggests that VVH may represent an earlier step in the evolution of Vibrio PFTs.

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Section: Resultsmentioning

confidence: 99%

Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family

Kaus

Lary

Cole

et al. 2014

Journal of Molecular Biology

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“…Nowadays, these assays are frequently used as a new approach to investigate in more detail the carbohydrate preferences of several CLRs [48][49][50]. However, one has to be cautious with the analysis of these data because spatial arrangement plays a prominent role in binding.…”

Section: Carbohydrate Recognition Domain (Crd)mentioning

confidence: 99%

C-Type Lectins on Dendritic Cells and Their Interaction with Pathogen-Derived and Endogenous Glycoconjugates

Gijzen¹,

Cambi²,

Torensma

et al. 2006

CPPS

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Human C-type lectin receptors (CLRs) characteristically bind glycosylated ligands in a Ca(2+)-dependent way via their carbohydrate recognition domain (CRD). Their carbohydrate preference is dependent on the amino acid sequence in the CRD domain and on the ability and flexibility of the CRD domain to accommodate sugar moieties that are located at different distances from each other in the glycoconjugate. Although microbial and vertebrate cells are able to produce similar polysaccharide chains, the density of carbohydrates on microbes is much higher compared to vertebrate cells. Despite this difference, carbohydrates present on both cell types can be recognized by the CLRs. These receptors are predominantly expressed by antigen presenting cells such as dendritic cells. In addition to the Toll-like receptor family, CLRs function as pattern recognition receptors by recognizing glycosylated patterns on pathogens. This usually results in internalization of the pathogen, lysosomal degradation and subsequent loading of pathogen-derived peptides into major histocompatibility complex molecules for antigen presentation. However, several pathogens have developed ways to exploit the CLRs to evade immune eradication by for example escaping from the lysosomal degradation pathway or by inducing anti-inflammatory cytokines. When CLRs bind endogenous glycosylated ligands they mediate several processes like cell-cell adhesion and clearance of aberrant cells like tumor cells or apoptotic cells.

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“…The task of defining the specificities of GBPs has been greatly helped by glycan array technology ( Blixt et al, 2004 ; Culf, Cuperlovic-Culf, & Ouellette, 2006 ; Drickamer & Taylor, 2002 ; Liu, Palma, & Feizi, 2009 ; Stevens, Blixt, Paulson, & Wilson, 2006 ). A glycan array is the reverse of a lectin array; it holds immobilized glycans to be probed by GBPs.…”

Section: Introductionmentioning

confidence: 99%

The Detection and Discovery of Glycan Motifs in Biological Samples Using Lectins and Antibodies: New Methods and Opportunities

Tang¹,

Hsueh²,

Kletter³

et al. 2015

Advances in Cancer Research

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Recent research is uncovering unexpected ways that glycans contribute to biology, as well as new strategies for combatting disease using approaches involving glycans. To make full use of glycans for clinical applications, we need more detailed information on the location, nature, and dynamics of glycan expression in vivo. Such studies require the use of specimens acquired directly from patients. Effective studies of clinical specimens require low-volume assays, high precision measurements, and the ability to process many samples. Assays using affinity reagents—lectins and glycan-binding antibodies—can meet these requirements, but further developments are needed to make the methods routine and effective. Recent advances in the use of glycan-binding proteins could meet that need. The advances involve improved determination of specificity using glycan arrays; the availability of databases for mining and analyzing glycan array data; lectin engineering methods; and the ability to quantitatively interpret lectin measurements. Here we describe many of the challenges and opportunities involved in the application of these new approaches to the study of biological samples. The new tools hold promise for developing methods to improve the outcomes of patients afflicted with diseases characterized by aberrant glycan expression.

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Abstract: Two recent papers describe how arrays of oligosaccharide and polysaccharide molecules can be used to investigate the interactions between carbohydrates and proteins more fully.

Cited by 68 publications

References 7 publications

Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family

Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family

C-Type Lectins on Dendritic Cells and Their Interaction with Pathogen-Derived and Endogenous Glycoconjugates

The Detection and Discovery of Glycan Motifs in Biological Samples Using Lectins and Antibodies: New Methods and Opportunities

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