Lectins: Carbohydrate-specific Reagents and Biological Recognition Molecules

Sharon, Nathan

doi:10.1074/jbc.x600004200

Cited by 406 publications

(271 citation statements)

References 115 publications

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“…Like antibodies, some lectins are known to play important roles in the immune system including defense against invading microorganisms and modulation of inflammatory and autoreactive processes through specific recognition of cellular and/or bacterial surface saccharide moieties. These characteristics make lectins very useful for glycoanalysis and medicine development 16, 17, 18, 19, 20, 21. Due to their minimization of sample consumption and high throughput format for analyzing multiple targets simultaneously, lectin microarrays have been employed in the glycomics study 22, 23, 24, 25, 26.…”

Section: Introductionmentioning

confidence: 99%

Uncovering the Binding Specificities of Lectins with Cells for Precision Colorectal Cancer Diagnosis Based on Multimodal Imaging

et al. 2018

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There is a high desire for novel targets/biomarkers to diagnose and treat colorectal cancer (CRC). Here, an approach starting from a polyacrylamide hydrogel–based lectin microarray is presented to screen the high expression of glycans on the CRC cell surface and to identify new lectin biomarkers for CRC. Three common CRC cell lines (SW480, SW620, and HCT116) and one normal colon cell line (NCM460) are profiled on the microarray with 27 lectins. The experimental results reveal that CRC cells highly express the glycans with d‐galactose, d‐glucose, and/or sialic acid residues, and Uelx Europaeus Agglutinin‐I (UEA‐I) exhibits reasonable specificity with SW480 cells. After conjugation of UEA‐I with silica‐coated NaGdF4:Yb3+, Er3+@NaGdF4 upconversion nanoparticles, the follow‐up in vitro and in vivo experiments provide further evidence on that UEA‐I can serve as tumor‐targeting molecule to diagnose SW480 tumor by multimodal imaging including upconversion luminescence imaging, T 1‐weighted magnetic resonance imaging, and X‐ray computed tomography imaging.

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Section: Introductionmentioning

confidence: 99%

Uncovering the Binding Specificities of Lectins with Cells for Precision Colorectal Cancer Diagnosis Based on Multimodal Imaging

et al. 2018

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“…Little is known concerning the arrangement of carbohydrate molecules on the surfaces of the different developmental stages of the fungus, although such changes may have important consequences regarding adhesion, host detection, cuticle penetration and non-self recognition by host defence mechanisms. Lectins represent relatively simple probes for the identification of specific carbohydrate residues on the surfaces of cells, and have been extensively used to characterize fungal cell walls, including particularly the examination of host-pathogen interactions (Lis & Sharon, 1986;Sharon & Lis, 1993;Sharon, 2007). Differences in surface constituents during fungal growth and among various developmental stages may influence host-parasite interactions, and alternations in surface mannose, glucose and sialic acid epitopes in Candida albicans and Aspergillus fumigatus have been linked to their ability to infect and colonize hosts as well as to activate immune cells and cytokine production (Esquenazi et al, 2003;Latgé et al, 1994;Masuoka, 2004;Warwas et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Lectin mapping reveals stage-specific display of surface carbohydrates in in vitro and haemolymph-derived cells of the entomopathogenic fungus Beauveria bassiana

2009

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The entomopathogenic fungus Beauveria bassiana and its insect host target represent a model system with which to examine host–pathogen interactions. Carbohydrate epitopes on the surfaces of fungal cells play diverse roles in processes that include adhesion, non-self recognition and immune invasion with respect to invertebrate hosts. B. bassiana produces a number of distinct cell types that include aerial conidia, submerged conidia, blastospores and haemolymph-derived cells termed in vivo blastospores or hyphal bodies. In order to characterize variations in the surface carbohydrate epitopes among these cells, a series of fluorescently labelled lectins, combined with confocal microscopy and flow cytometry to quantify the response, was used. Aerial conidia displayed the most diverse lectin binding characteristics, showing reactivity against concanavalin A (ConA), Galanthus nivalis (GNL), Griffonia simplicifolia (GSII), Helix pomatia (HPA), Griffonia simplicifolia isolectin (GSI), peanut agglutinin (PNA), Ulex europaeus agglutinin I (UEAI) and wheatgerm agglutinin (WGA), and weak reactivity against Ricinus communis I (RCA), Sambucus nigra (SNA), Limax flavus (LFA) and Sophora japonica (SJA) lectins. Lectin binding to submerged conidia was similar to that to aerial conidia, except that no reactivity against UEAI, HPA and SJA was noted, and WGA appeared to bind strongly at specific polar spots. In contrast, the majority of in vitro blastospores were not bound by ConA, GNL, GSII, GSI, SNA, UEAI, LFA or SJA, with PNA binding in large patches, and some polarity in WGA binding noted. Significant changes in lectin binding also occurred after aerial conidial germination and in cells grown on either lactose or trehalose. For germinated conidia, differential lectin binding was noted between the conidial base, the germ tube and the hyphal tip. Fungal cells isolated from the haemolymph of the infected insect hosts Manduca sexta and Heliothis virescens appeared to shed most carbohydrate epitopes, displaying binding only to the GNL, PNA and WGA lectins. Ultrastructural examination of the haemolymph-derived cells revealed the presence of a highly ordered outermost brush-like structure not present on any of the in vitro cells. Haemolymph-derived hyphal bodies placed into rich broth medium showed expression of several surface carbohydrate epitopes, most notably showing increased PNA binding and strong binding by the RCA lectin. These data indicate robust and diverse production of carbohydrate epitopes on different developmental stages of fungal cells and provide evidence that surface carbohydrates are elaborated in infection-specific patterns.

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“…These proteins all display <10% sequence identity with BsCBM66, and the ligandbinding residues (see below) are not conserved in the three other proteins. It is unlikely, therefore, that these structural homologs of BsCBM66 will bind to fructans, although the two lectins are oligomeric and thus display enhanced affinity through avidity affects (19,20).…”

Section: Resultsmentioning

confidence: 99%

How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity

Cuskin

Flint

Gloster

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

115

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Noncatalytic carbohydrate binding modules (CBMs) are components of glycoside hydrolases that attack generally inaccessible substrates. CBMs mediate a two-to fivefold elevation in the activity of endoacting enzymes, likely through increasing the concentration of the appended enzymes in the vicinity of the substrate. The function of CBMs appended to exo-acting glycoside hydrolases is unclear because their typical endo-binding mode would not fulfill a targeting role. Here we show that the Bacillus subtilis exo-acting β-fructosidase SacC, which specifically hydrolyses levan, contains the founding member of CBM family 66 (CBM66). The SacC-derived CBM66 (BsCBM66) targets the terminal fructosides of the major fructans found in nature. The crystal structure of BsCBM66 in complex with ligands reveals extensive interactions with the terminal fructose moiety (Fru-3) of levantriose but only limited hydrophobic contacts with Fru-2, explaining why the CBM displays broad specificity. Removal of BsCBM66 from SacC results in a ∼100-fold reduction in activity against levan. The truncated enzyme functions as a nonspecific β-fructosidase displaying similar activity against β-2,1-and β-2,6-linked fructans and their respective fructooligosaccharides. Conversely, appending BsCBM66 to BT3082, a nonspecific β-fructosidase from Bacteroides thetaiotaomicron, confers exolevanase activity on the enzyme. We propose that BsCBM66 confers specificity for levan, a branched fructan, through an "avidity" mechanism in which the CBM and the catalytic module target the termini of different branches of the same polysaccharide molecule. This report identifies a unique mechanism by which CBMs modulate enzyme function, and shows how specificity can be tailored by integrating nonspecific catalytic and binding modules into a single enzyme.isothermal titration calorimetry | X-ray crystallography | prebiotics | biofuels | lectins C omplex carbohydrates represent a major nutrient for numerous microbial ecosystems, exemplified by bacterial and fungal communities established in the rumen and large bowel of mammals, where they play an important role in animal nutrition and human health, respectively (1, 2). It is also evident that these composite structures are of increasing industrial significance, particularly in the bioenergy and bioprocessing sectors (3). The enzymes that catalyze the degradation of these complex carbohydrates, primarily glycoside hydrolases but also polysaccharide lyases, are grouped into sequence-based families on the continuously updated CAZy database (4). Members of the same family display a common fold, and the catalytic mechanism and catalytic apparatus are also conserved (5). Substrate specificity within glycoside hydrolase families (GHs), however, can vary significantly (6). Glycanases that attack inaccessible substrates often contain noncatalytic carbohydrate binding modules (CBMs; see ref. 7 for review) that are also grouped into sequence-based families in the CAZy database. Against recalcitrant substrates, CBMs enhance the activit...

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Lectins: Carbohydrate-specific Reagents and Biological Recognition Molecules

Cited by 406 publications

References 115 publications

Uncovering the Binding Specificities of Lectins with Cells for Precision Colorectal Cancer Diagnosis Based on Multimodal Imaging

Uncovering the Binding Specificities of Lectins with Cells for Precision Colorectal Cancer Diagnosis Based on Multimodal Imaging

Lectin mapping reveals stage-specific display of surface carbohydrates in in vitro and haemolymph-derived cells of the entomopathogenic fungus Beauveria bassiana

How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity

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