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1. Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins

Author

Ana Gimeno, Jesús Jiménez-Barbero, Stefania Robakiewicz, Sandra Delgado, Clarisse Bridot, Begoña Echeverria, Ann Dansercoer, Nicola G. A. Abrescia, Jérôme de Ruyck, Sonia Serna, Shubham Semwal, Mikel Azkargorta, Ruud H. P. Wilbers, Ana Ardá, Savvas N. Savvides, Diego Charro, Niels C. Reichardt, Kenneth Verstraete, Julie Bouckaert, Kim van Noort, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Centro de Investigación Cooperativa en Biomateriales (CIC biomaGUNE), Cell Biology and Stem Cells Unit (CICbioGUNE), Technologic Park of Bizkaia, VIB-UGent Center for Inflammation Research [Gand, Belgique] (IRC), VIB [Belgium], Wageningen University and Research [Wageningen] (WUR), Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Instituto de Salud Carlos III [Madrid] (ISC)-ministerio de ciencia e innovacion, Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576, Centro de Investigación Cooperativa en Biomateriales [CIC biomaGUNE], Cell Biology and Stem Cells Unit [CICbioGUNE], VIB-UGent Center for Inflammation Research [Gand, Belgique] [IRC], Wageningen University and Research [Wageningen] [WUR], Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF], and Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine [CIBER-BBN]

Subjects
[SDV]Life Sciences [q-bio], Mannose, Biochemistry, Epitope, Epitopes, Mice, chemistry.chemical_compound, 0302 clinical medicine, Mannitou, N-linked glycosylation, BINDING, Medicine and Health Sciences, AFFINITY, Mammals, chemistry.chemical_classification, 0303 health sciences, biology, PROLIFERATION, paucimannosidic epitopes, Schistosoma mansoni, N-GLYCOSYLATION, CANCER, 3. Good health, DNA-Binding Proteins, GLYCAN MICROARRAYS, 030220 oncology & carcinogenesis, N-glycan, Antibody, Glycan, core fucose, IgM, CORE FUCOSYLATION, 03 medical and health sciences, Antigen, Polysaccharides, Animals, Humans, Laboratorium voor Nematologie, Fucose, Glycoproteins, 030304 developmental biology, Membrane Proteins, Biology and Life Sciences, IgM binding, Immunoglobulin M, chemistry, ANTIBODIES, biology.protein, Laboratory of Nematology, Glycoprotein, ELASTASE
Abstract

Paucimannosidic glycans are restricted to the core structure [Man1–3GlcNAc2Fuc0–1] of N-glycans and are rarely found in mammalian tissues. Yet, especially [Man2-3GlcNAc2Fuc1] have been found significantly upregulated in tumors, including in colorectal and liver cancer. Mannitou IgM is a murine monoclonal antibody that was previously shown to recognize Man3GlcNAc2 with an almost exclusive selectivity. Here, we have sought the definition of the minimal glycan epitope of Mannitou IgM, initiated by screening on a newly designed paucimannosidic glycan microarray; among the best binders were Man3GlcNAc2 and its α1,6 core-fucosylated variant, Man3GlcNAc2Fuc1. Unexpectedly and in contrast to earlier findings, Man5GlcNAc2-type structures bind equally well and a large tolerance was observed for substitutions on the α1,6 arm. It was confirmed that any substitution on the single α1,3-linked mannose completely abolishes binding. Surface plasmon resonance for kinetic measurements of Mannitou IgM binding, either directly on the glycans or as presented on omega-1 and kappa-5 soluble egg antigens from the helminth parasite Schistosoma mansoni, showed submicromolar affinities. To characterize the epitope in greater and atomic detail, saturation transfer difference nuclear magnetic resonance spectroscopy was performed with the Mannitou antigen-binding fragment. The STD-NMR data demonstrated the strongest interactions with the aliphatic protons H1 and H2 of the α1–3-linked mannose and weaker imprints on its H3, H4 and H5 protons. In conclusion, Mannitou IgM binding requires a nonsubstituted α1,3-linked mannose branch of paucimannose also on proteins, making it a highly specific tool for the distinction of concurrent human tumor-associated carbohydrate antigens.

Published
2021
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2. TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions

Author

Sabine Mayer-Lambertz, Corinne Vivès, Bernd Lepenies, Franck Fieschi, João T. Monteiro, Christine Ebel, Michel Thépaut, Niels-Christian Reichardt, Aline Le Roy, Sonia Serna, Silvia Achilli, Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Immunology Unit and Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, CIC biomaGUNE, Glycotechnology Laboratory, Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Instituto de Salud Carlos III [Madrid] (ISC)-ministerio de ciencia e innovacion, Department of Biomolecular Systems [Potsdam], Max Planck Institute of Colloids and Interfaces, Max-Planck-Gesellschaft-Max-Planck-Gesellschaft, and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
0301 basic medicine, Glycan, Recombinant Fusion Proteins, glycan array, Ligands, 01 natural sciences, Catalysis, Article, Flow cytometry, law.invention, lcsh:Chemistry, Inorganic Chemistry, 03 medical and health sciences, C-type lectin, Confocal microscopy, law, Candida albicans, medicine, pathogen recognition, Lectins, C-Type, Physical and Theoretical Chemistry, Receptor, lcsh:QH301-705.5, Molecular Biology, Spectroscopy, biology, medicine.diagnostic_test, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], 010405 organic chemistry, Chemistry, Organic Chemistry, Lectin, General Medicine, multivalency, Ligand (biochemistry), Flow Cytometry, In vitro, eye diseases, 0104 chemical sciences, Computer Science Applications, Immunoglobulin Fc Fragments, DC-SIGNR, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Biochemistry, biology.protein
Abstract

International audience; C-type lectin receptor (CLR)/carbohydrate recognition occurs through low affinity interactions. Nature compensates that weakness by multivalent display of the lectin carbohydrate recognition domain (CRD) at the cell surface. Mimicking these low affinity interactions in vitro is essential to better understand CLR/glycan interactions. Here, we present a strategy to create a generic construct with a tetrameric presentation of the CRD for any CLR, termed TETRALEC. We applied our strategy to a naturally occurring tetrameric CRD, DC-SIGNR, and compared the TETRALEC ligand binding capacity by synthetic N- and O-glycans microarray using three different DC-SIGNR constructs i) its natural tetrameric counterpart, ii) the monomeric CRD and iii) a dimeric Fc-CRD fusion. DC-SIGNR TETRALEC construct showed a similar binding profile to that of its natural tetrameric counterpart. However, differences observed in recognition of low affinity ligands underlined the importance of the CRD spatial arrangement. Moreover, we further extended the applications of DC-SIGNR TETRALEC to evaluate CLR/pathogens interactions. This construct was able to recognize heat-killed Candida albicans by flow cytometry and confocal microscopy, a so far unreported specificity of DC-SIGNR. In summary, the newly developed DC-SIGNR TETRALEC tool proved to be useful to unravel novel CLR/glycan interactions, an approach which could be applied to other CLRs.

Published
2020
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3. Chemoenzymatic Synthesis of N-glycan Positional Isomers and Evidence for Branch Selective Binding by Monoclonal Antibodies and Human C-type Lectin Receptors

Author

Michel Thépaut, Cornelis H. Hokke, Begoña Echeverria, Niels-Christian Reichardt, Julie Pham, Silvia Achilli, Sonia Serna, Corinne Vivès, Franck Fieschi, CIC biomaGUNE, Glycotechnology Laboratory, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Department of Parasitology, Leiden University Medical Center (LUMC), Universiteit Leiden-Universiteit Leiden, Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Instituto de Salud Carlos III [Madrid] (ISC)-ministerio de ciencia e innovacion, Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Glycan, medicine.drug_class, Receptors, Cell Surface, Monoclonal antibody, 01 natural sciences, Biochemistry, 03 medical and health sciences, Mice, Isomerism, C-type lectin, Polysaccharides, Structural isomer, medicine, Animals, Humans, Lectins, C-Type, Receptor, Innate immune system, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], 010405 organic chemistry, Chemistry, Lectin, Antibodies, Monoclonal, General Medicine, 0104 chemical sciences, carbohydrates (lipids), 030104 developmental biology, Receptors, Mitogen, biology.protein, Biocatalysis, Molecular Medicine, Antibody, Cell Adhesion Molecules
Abstract

Here, we describe a strategy for the rapid preparation of pure positional isomers of complex N-glycans to complement an existing array comprising a larger number of N-glycans and smaller glycan structures. The expanded array was then employed to study context-dependent binding of structural glycan fragments by monoclonal antibodies and C-type lectins. A partial enzymatic elongation of semiprotected core structures was combined with the protecting-group-aided separation of positional isomers by preparative HPLC. This methodology, which avoids the laborious chemical differentiation of antennae, was employed for the preparation of eight biantennary N-glycans with Galβ1,4GlcNAc (LN), GalNAcβ1,4GlcNAc (LDN), and GalNAcβ1,4[Fucα1,3]GlcNAc (LDNF) motifs presented on either one or both antennae. Screening of the binding specificities of three anti-LeX monoclonal IgM antibodies raised against S. mansoni glycans and three C-type lectin receptors of the innate immune system, namely DC-SIGN, DC-SIGNR, and LSECtin, revealed a surprising context-dependent fine specificity for the recognition of the glycan motifs. Moreover, we observed a striking selection of one individual positional isomer over the other by the C-type lectins tested, underscoring the biological relevance of the structural context of glycan elements in molecular recognition.

Published
2018
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