Allosteric Regulation of the Carbohydrate-binding Ability of a Novel Conger Eel Galectin by d-Mannoside

Watanabe, Mizuki; Nakamura, Osamu; Muramoto, Koji; Ogawa, Tomoya

doi:10.1074/jbc.m112.346213

Cited by 16 publications

(9 citation statements)

References 40 publications

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“…In the conger eel ( Congeer myriaster ) both isotypes of congerin, a proto-type galectin, participate in cellular encapsulation of the parasitic nematode ( Cucullanus spp.) via the induction of cellular adhesion to the parasites through galectin-glycan recognition (Nakamura et al 2012; Watanabe et al 2012). Other examples have revealed direct and specific interactions of fish galectins with the pathogens (Tasumi et al 2002; Tanguy et al 2004; Dutta et al 2005) and by controlling virulence and viral replication rate by modulating the viral adhesion to the host (Poisa-Beiro et al 2009; Liu, S. et al 2013).…”

Section: Discussionmentioning

confidence: 99%

The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells

Niță-Lazăr

Mancini

Feng

et al. 2016

Developmental & Comparative Immunology

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The infectious hematopoietic necrosis virus (IHNV; Rhabdoviridae, Novirhabdovirus) infects teleost fish, such as salmon and trout, and is responsible for significant losses in the aquaculture industry and in wild fish populations. Although IHNV enters the host through the skin at the base of the fins, the viral adhesion and entry mechanisms are not fully understood. In recent years, evidence has accumulated in support of the key roles played by protein-carbohydrate interactions between host lectins secreted to the extracellular space and virion envelope glycoproteins in modulating viral adhesion and infectivity. In this study, we assessed in vitro the potential role(s) of zebrafish (Danio rerio) proto type galectin-1 (Drgal1-L2) and a chimera galectin-3 (Drgal3-L1) in IHNV adhesion to epithelial cells. Our results suggest that the extracellular Drgal1-L2 and Drgal3-L1 interact directly and in a carbohydrate-dependent manner with the IHNV glycosylated envelope and glycans on the epithelial cell surface, significantly reducing viral adhesion.

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Section: Discussionmentioning

confidence: 99%

The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells

Niță-Lazăr

Mancini

Feng

et al. 2016

Developmental & Comparative Immunology

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“…This study part thus provides no evidence for a galectin-like reactivity to a common glycan, tested either with glycocompounds or glycosylation mutants as ligands (microarray, cell assay) or inhibitor (cell assay). Also, the cell assays in the presence of glycans exclude the possibility of an allosteric activation of lactose binding by the test substances, revealed previously for mannose in the case of the mentioned congerin P [50]. In consequence, C-GRP appears to have lost lectin activity despite the presence of the central Trp residue, which separates avian from mammalian GRP (Fig.…”

Section: C-grp On the Level Of The Proteinmentioning

confidence: 52%

“…Of note, deviations in positions of the signature sequence do not necessarily mean that a member of this family will lose its lectin activity. In the cases of congerin P, the galectin of peritoneal cells of the conger eel [50], and the third protein of the galectin family in the inky cap mushroom Coprinopsis cinerea termed CGL3 [51], glycan binding is still operative despite such alterations. These precedents prompted us to perform further assays using a microarray and cytofluorimetry of cells with defined changes in their surface glycomes.…”

Section: C-grp On the Level Of The Proteinmentioning

confidence: 99%

Galectin-related protein: An integral member of the network of chicken galectins 1. From strong sequence conservation of the gene confined to vertebrates to biochemical characteristics of the chicken protein and its crystal structure

Caballero

Flores-Ibarra

Michalak

et al. 2016

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Endogenous lectins are multifunctional effectors in cell physiology. Adding the sixth member of the galectin family in chicken, a model organism for systematic profiling of these adhesion/growth-regulatory proteins, is a step toward comprehensive network monitoring. Methods: Database mining and computational data processing are applied for gene detection, chromosomal location and sequence alignments. Cloning, recombinant production and fusion-protein technology gain access to the protein, mass spectrometry and gel electrophoresis/filtration provide analytical data. Haemagglutination, glycan microarray and cell assays assess binding capacity, and crystallography of a shortened variant (also analyzed by ultracentrifugation and small angle X-ray scattering) determines its structure. Results: The gene for the galectin-related protein (GRP) is present exclusively in vertebrates with high-level sequence conservation and similar chromosomal positioning. The chicken protein is monomeric and has lost the canonical galectin property of binding lactose. The crystal structure of the variant without the 36-amino-acid extension at the start provides explanations for this lack of binding. Conclusions: Chicken GRP is special within this family of six proteins by being unable to bind lactose. The documented high degree of sequence conservation among vertebrate orthologues confers the status of a model for delineating an assumedly shared functionality to this GRP. General significance: Biochemical characterization of a product of a gene under strong positive selection is a prerequisite for functional characterization. It is also essential for network monitoring by adding a new member to this lectin family.

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“…Griffonia simplifolia (GSL-II) [53] Wisteria floribunda (WFA) [59] VIP36 [60] Fungal galectin (ACG) [62] Mutants of nematode galectin LEC-6 [63] Conger eel (congerin P) [64] Marine sponge Halichondria okadai [65] Nematode gene DC2.3 [66] Mutants of ACG [67] Two lectin domains of nematode galectin LEC-1 [68] Human galectins 1-9 and other lectins [38] Nematode galectins [69,70] American bullfrog Rna catesbeiana [71] Cysteine-less mutant of human galectin-1 [72] Nematode galectin (LEC-6) [73] Nematode galectins (LEC-1~LEC-11) [74] Human galectins [75] Marine sponge Halichondria okadai [76] Mutants of nematode galectin (LEC-1) [77] Human galectin-9 N-terminal CRD [78] The nematode galectin LEC-1 and its mutants [79] Argasid tick Ornithodoros moubata.…”

Section: Erythrina Species [58]mentioning

confidence: 99%

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

et al. 2015

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Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms-from humans to microorganisms, including viruses-and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin's function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named "Lectin frontier DataBase (LfDB)", which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd's). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. OPEN ACCESS

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Allosteric Regulation of the Carbohydrate-binding Ability of a Novel Conger Eel Galectin by d-Mannoside

Cited by 16 publications

References 40 publications

The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells

The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells

Galectin-related protein: An integral member of the network of chicken galectins 1. From strong sequence conservation of the gene confined to vertebrates to biochemical characteristics of the chicken protein and its crystal structure

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

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