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5. Involvement of Surfactant Protein D in Ebola Virus Infection Enhancement via Glycoprotein Interaction

Author

Favier, Anne-Laure, Reynard, Olivier, Gout, Evelyne, Van Eijk, Martin, Haagsman, Henk, Crouch, Erika, Volchkov, Viktor, Peyrefitte, Christophe, and Thielens, Nicole

Subjects
Quantitative Biology - Biomolecules
Abstract

Since the largest 2014-2016 Ebola virus disease outbreak in West Africa, understanding of Ebola virus infection has improved, notably the involvement of innate immune mediators. Amongst them, collectins are important players in the antiviral innate immune defense. A screening of Ebola glycoprotein (GP)-collectins interactions revealed the specific interaction of human surfactant protein D (hSP-D), a lectin expressed in lung and liver, two compartments where Ebola was found in vivo. Further analyses have demonstrated an involvement of hSP-D in the enhancement of virus infection in several in vitro models. Similar effects were observed for porcine SP-D (pSP-D). In addition, both hSP-D and pSP-D interacted with Reston virus (RESTV) GP and enhanced pseudoviral infection in pulmonary cells. Thus, our study reveals a novel partner of Ebola GP that may participate to enhance viral spread.

Published
2019
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9. Glycosaminoglycans Exhibit Distinct Interactions and Signaling with Bmp2 According to Their Nature and Localization

Author

Le Pennec, Jean, primary, Makshakova, Olga N., additional, Nevola, Paola, additional, Fouladkar, Farah, additional, Gout, Evelyne, additional, Machillot, Paul, additional, Friedel-Arboleas, Mélanie, additional, Picart, Catherine, additional, Perez, Serge, additional, Vortkamp, Andrea, additional, Vivès, Romain R., additional, and Migliorini, Elisa, additional

Published
2024
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14. Preparation and Characterization of Heparan Sulfate-Derived to Investigate Protein–GAG Interaction and HS Enzyme Activity

Author

Laguri, Cédric, Sadir, Rabia, Gout, Evelyne, Vivès, Romain, Lortat-Jacob, Hugues, 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)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

Subjects
Chemoenzymatic approaches, Heparan sulfate, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, NMR-based structural studies, Protein–heparan sulfate interaction, HPLC disaccharide analysis, Glycosaminoglycans
Abstract

International audience; Heparan sulfate chains are complex and structurally diverse polysaccharides that interact with a large number of proteins, thereby regulating a vast array of biological functions. Understanding this activity requires obtaining oligosaccharides of defined structures. Here we describe methods for isolating, engineering, and characterizing heparan sulfate-derived oligosaccharides and approaches based on high-performance liquid chromatography (HPLC), nuclear magnetic resonance (NMR), and bio-layer interferometry (BLI) to study their structures, modifications, and interactions.

Published
2022
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15. Elicitation of potent SARS-CoV-2 neutralizing antibody responses through immunization with a versatile adenovirus-inspired multimerization platform

Author

Chevillard, Christopher, primary, Amen, Axelle, additional, Besson, Solène, additional, Hannani, Dalil, additional, Bally, Isabelle, additional, Dettling, Valentin, additional, Gout, Evelyne, additional, Moreau, Christophe J., additional, Buisson, Marlyse, additional, Gallet, Salomé, additional, Fenel, Daphna, additional, Vassal-Stermann, Emilie, additional, Schoehn, Guy, additional, Poignard, Pascal, additional, Dagher, Marie-Claire, additional, and Fender, Pascal, additional

Published
2022
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16. Extracellular endosulfatase Sulf-2 harbors a chondroitin/dermatan sulfate chain that modulates its enzyme activity

Author

El Masri, Rana, primary, Seffouh, Amal, additional, Roelants, Caroline, additional, Seffouh, Ilham, additional, Gout, Evelyne, additional, Pérard, Julien, additional, Dalonneau, Fabien, additional, Nishitsuji, Kazuchika, additional, Noborn, Fredrik, additional, Nikpour, Mahnaz, additional, Larson, Göran, additional, Crétinon, Yoann, additional, Friedel-Arboleas, Mélanie, additional, Uchimura, Kenji, additional, Daniel, Régis, additional, Lortat-Jacob, Hugues, additional, Filhol, Odile, additional, and Vivès, Romain R., additional

Published
2022
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18. Discrimination of deletion to point cytokine mutants based on an array of cross-reactive receptors mimicking protein recognition by heparan sulfate

Author

Genua, Maria, primary, Garçon, Laurie-Amandine, additional, Sergeeva, Yulia N., additional, Saesen, Els, additional, Musnier, Benjamin, additional, Buhot, Arnaud, additional, Billon, Martial, additional, Gout, Evelyne, additional, Sadir, Rabia, additional, Lortat-Jacob, Hugues, additional, Le Narvor, Christine, additional, Bonnaffé, David, additional, Livache, Thierry, additional, and Hou, Yanxia, additional

Published
2021
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19. Preparation and characterization of Heparan sulfate derived oligosaccharides to investigate protein-GAG interaction and HS biosynthesis enzyme activity

Author

Laguri, Cédric, Sadir, Rabia, Gout, Evelyne, Vives, R.R., Lortat-Jacob, Hugues, 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), and Lortat-Jacob, Hugues

Subjects
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2021

20. Extracellular endosulfatase Sulf-2 harbours a chondroitin/dermatan sulfate chain that modulates its enzyme activity

Author

Masri, Rana El, primary, Seffouh, Amal, additional, Roelants, Caroline, additional, Seffouh, Ilham, additional, Gout, Evelyne, additional, Pérard, Julien, additional, Dalonneau, Fabien, additional, Nishitsuji, Kazuchika, additional, Noborn, Fredrik, additional, Nikpour, Mahnaz, additional, Larson, Göran, additional, Crétinon, Yoann, additional, Uchimura, Kenji, additional, Daniel, Régis, additional, Lortat-Jacob, Hugues, additional, Filhol, Odile, additional, and Vivès, Romain R., additional

Published
2021
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21. Extracellular Endosulfatase Sulf-2 Harbours a Chondroitin/Dermatan Sulfate Chain That Modulates Its Enzyme Activity

Author

El Masri, Rana, primary, Seffouh, Amal, additional, Roelants, Caroline, additional, Seffouh, Ilham, additional, Gout, Evelyne, additional, Pérard, Julien, additional, Dalonneau, Fabien, additional, Nishitsuji, Kazuchika, additional, Noborn, Fredrik, additional, Nikpour, Mahnaz, additional, Larson, Goran, additional, Crétinon, Yoann, additional, Uchimura, Kenji, additional, Daniel, Régis, additional, Lortat-Jacob, Hugues, additional, Filhol, Odile, additional, and Vivès, Romain R., additional

Published
2021
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22. Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases

Author

Galinier, Richard, Gout, Evelyne, Lortat-Jacob, Hugues, Wood, Jonathan, and Chroboczek, Jadwiga

Subjects
Biochemistry -- Research, Adenoviruses -- Physiological aspects, Proteins -- Physiological aspects, Ligases -- Physiological aspects, Ubiquitin -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on adenovirus penton base protein. The study of the cellular partners of this protein has been carried out via dodecahedra used for human lung expression library screening, and the results indicate that the screen has yielded ubiquitin-protein ligases which belong to Nedd4-like group of E3 enzymes.

Published
2002

23. Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases

Author

Fouët, Guillaume, primary, Gout, Evelyne, additional, Wicker-Planquart, Catherine, additional, Bally, Isabelle, additional, De Nardis, Camilla, additional, Dedieu, Stéphane, additional, Chouquet, Anne, additional, Gaboriaud, Christine, additional, Thielens, Nicole M., additional, Kleman, Jean-Philippe, additional, and Rossi, Véronique, additional

Published
2020
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27. Involvement of Surfactant Protein D in Ebola Virus Infection Enhancement via Glycoprotein Interaction

Author

Favier, Anne-Laure, Reynard, Olivier, Gout, Evelyne, van Eijk, Martin, Haagsman, Henk P, Crouch, Erika, Volchkov, Viktor, Peyrefitte, Christophe, Thielens, Nicole M, Favier, Anne-Laure, Reynard, Olivier, Gout, Evelyne, van Eijk, Martin, Haagsman, Henk P, Crouch, Erika, Volchkov, Viktor, Peyrefitte, Christophe, and Thielens, Nicole M

Abstract

Since the largest 2014⁻2016 Ebola virus disease outbreak in West Africa, understanding of Ebola virus infection has improved, notably the involvement of innate immune mediators. Amongst them, collectins are important players in the antiviral innate immune defense. A screening of Ebola glycoprotein (GP)-collectins interactions revealed the specific interaction of human surfactant protein D (hSP-D), a lectin expressed in lung and liver, two compartments where Ebola was found in vivo. Further analyses have demonstrated an involvement of hSP-D in the enhancement of virus infection in several in vitro models. Similar effects were observed for porcine SP-D (pSP-D). In addition, both hSP-D and pSP-D interacted with Reston virus (RESTV) GP and enhanced pseudoviral infection in pulmonary cells. Thus, our study reveals a novel partner of Ebola GP that may participate to enhance viral spread.

Published
2018

28. Involvement of Surfactant Protein D in Ebola Virus Infection Enhancement via Glycoprotein Interaction

Author

LS Moleculaire Afweer, dI&I I&I-3, Dep Infectieziekten Immunologie, Favier, Anne-Laure, Reynard, Olivier, Gout, Evelyne, van Eijk, Martin, Haagsman, Henk P, Crouch, Erika, Volchkov, Viktor, Peyrefitte, Christophe, Thielens, Nicole M, LS Moleculaire Afweer, dI&I I&I-3, Dep Infectieziekten Immunologie, Favier, Anne-Laure, Reynard, Olivier, Gout, Evelyne, van Eijk, Martin, Haagsman, Henk P, Crouch, Erika, Volchkov, Viktor, Peyrefitte, Christophe, and Thielens, Nicole M

Published
2018

29. Autoantibodies Targeting Ficolin-2 in Systemic Lupus Erythematosus Patients With Active Nephritis

Author

Colliard, Sophie, primary, Jourde-Chiche, Noémie, additional, Clavarino, Giovanna, additional, Sarrot-Reynauld, Françoise, additional, Gout, Evelyne, additional, Deroux, Alban, additional, Fougere, Mélanie, additional, Bardin, Nathalie, additional, Bouillet, Laurence, additional, Cesbron, Jean-Yves, additional, Thielens, Nicole M., additional, and Dumestre-Pérard, Chantal, additional

Published
2018
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30. Interaction of Complement Defence Collagens C1q and Mannose-Binding Lectin with BMP-1/Tolloid-like Proteinases

Author

Lacroix, Monique, primary, Tessier, Agnès, additional, Dumestre-Pérard, Chantal, additional, Vadon-Le Goff, Sandrine, additional, Gout, Evelyne, additional, Bruckner-Tuderman, Leena, additional, Kiritsi, Dimitra, additional, Nyström, Alexander, additional, Ricard-Blum, Sylvie, additional, Moali, Catherine, additional, Hulmes, David J. S., additional, and Thielens, Nicole M., additional

Published
2017
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32. Molecular dissection of the interaction of C1q with CD91

Author

Bally, Isabelle, primary, Gout, Evelyne, additional, Wicker-Planquart, Catherine, additional, Chouquet, Anne, additional, Frachet, Philippe, additional, Thielens, Nicole M., additional, Kleman, Jean-Philippe, additional, and Rossi, Véronique, additional

Published
2016
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33. Association between the Presence of Autoantibodies Targeting Ficolin-3 and Active Nephritis in Patients with Systemic Lupus Erythematosus

Author

Plawecki, Maëlle, primary, Lheritier, Elise, additional, Clavarino, Giovanna, additional, Jourde-Chiche, Noémie, additional, Ouili, Saber, additional, Paul, Stéphane, additional, Gout, Evelyne, additional, Sarrot-Reynauld, Françoise, additional, Bardin, Nathalie, additional, Boëlle, Pierre -Yves, additional, Chiche, Laurent, additional, Bouillet, Laurence, additional, Thielens, Nicole M., additional, Cesbron, Jean-Yves, additional, and Dumestre-Pérard, Chantal, additional

Published
2016
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35. Human L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic acid

Author

Vassal-Stermann, Emilie, Lacroix, Monique, Gout, Evelyne, Laffly, Emmanuelle, Pedersen, Christian Marcus, Martin, Lydie, Amoroso, Ana, Schmidt, Richard R., Zähringer, Ulrich, Gaboriaud, Christine, Guilmi, Anne Marie Di, Thielens, Nicole M., Vassal-Stermann, Emilie, Lacroix, Monique, Gout, Evelyne, Laffly, Emmanuelle, Pedersen, Christian Marcus, Martin, Lydie, Amoroso, Ana, Schmidt, Richard R., Zähringer, Ulrich, Gaboriaud, Christine, Guilmi, Anne Marie Di, and Thielens, Nicole M.

Abstract

Human L-ficolin is a soluble protein of the innate immune system able to sense pathogens through its fibrinogen (FBG) recognition domains and to trigger activation of the lectin complement pathway through associated serine proteases. L-Ficolin has been previously shown to recognize pneumococcal clinical isolates, but its ligands and especially its molecular specificity remain to be identified. Using solid-phase binding assays, serum and recombinant L-ficolins were shown to interact with serotype 2 pneumococcal strain D39 and its unencapsulated R6 derivative. Incubation of both strains with serum triggered complement activation, as measured by C4b and C3b deposition, which was decreased by using ficolin-depleted serum. Recombinant L-ficolin and its FBG-like recognition domain bound to isolated pneumococcal cell wall extracts, whereas binding to cell walls depleted of teichoic acid (TA) was decreased. Both proteins were also shown to interact with two synthetic TA compounds, each comprising part structures of the complete lipoteichoic acid molecule with two PCho residues. Competition studies and direct interaction measurements by surface plasmon resonance identified PCho as a novel L-ficolin ligand. Structural analysis of complexes of the FBG domain of L-ficolin and PCho revealed that the phosphate moiety interacts with amino acids previously shown to define an acetyl binding site. Consequently, binding of L-ficolin to immobilized acetylated BSA was inhibited by PCho and synthetic TA. Binding of serum L-ficolin to immobilized synthetic TA and PCho-conjugated BSA triggered activation of the lectin complement pathway, thus further supporting the hypothesis of L-ficolin involvement in host antipneumococcal defense.

Published
2014

36. Human L-Ficolin Recognizes Phosphocholine Moieties of Pneumococcal Teichoic Acid

Author

Vassal-Stermann, Emilie, primary, Lacroix, Monique, additional, Gout, Evelyne, additional, Laffly, Emmanuelle, additional, Pedersen, Christian M., additional, Martin, Lydie, additional, Amoroso, Ana, additional, Schmidt, Richard R., additional, Zähringer, Ulrich, additional, Gaboriaud, Christine, additional, Di Guilmi, Anne-Marie, additional, and Thielens, Nicole M., additional

Published
2014
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37. Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin

Author

Gout, Evelyne, Garlatti, Virginie, Smith, David F, Lacroix, Monique, Dumestre-Pérard, Chantal, Lunardi, Thomas, Martin, Lydie, Cesbron, Jean-Yves, Arlaud, Gérard J, Gaboriaud, Christine, Thielens, Nicole, Institut de biologie structurale (IBS - UMR 5075 ), 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)-Centre National de la Recherche Scientifique (CNRS), Department of Biochemistry, Emory University [Atlanta, GA], Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Carbohydrates, Mutation, Missense, Protein Array Analysis, Glycobiology and Extracellular Matrices, Crystallography, X-Ray, MESH: Tyrosine, MESH: Lectins, Polysaccharides, Lectins, MESH: Protein Binding, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Mutation, Missense, MESH: Humans, MESH: Protein Array Analysis, Fibrinogen, MESH: Crystallography, X-Ray, N-Acetylneuraminic Acid, MESH: Mutagenesis, Site-Directed, MESH: Polysaccharides, MESH: Fibrinogen, Mutagenesis, Site-Directed, Tyrosine, MESH: N-Acetylneuraminic Acid, MESH: Carbohydrates, Protein Binding
Abstract

International audience; Ficolins are oligomeric innate immune recognition proteins consisting of a collagen-like region and a fibrinogen-like recognition domain that bind to pathogen- and apoptotic cell-associated molecular patterns. To investigate their carbohydrate binding specificities, serum-derived L-ficolin and recombinant H- and M-ficolins were fluorescently labeled, and their carbohydrate binding ability was analyzed by glycan array screening. L-ficolin preferentially recognized disulfated N-acetyllactosamine and tri- and tetrasaccharides containing terminal galactose or N-acetylglucosamine. Binding was sensitive to the position and orientation of the bond between N-acetyllactosamine and the adjacent carbohydrate. No significant binding of H-ficolin to any of the 377 glycans probed could be detected, providing further evidence for its poor lectin activity. M-ficolin bound preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. To further investigate the structural basis of sialic acid recognition by M-ficolin, point mutants were produced in which three residues of the fibrinogen domain were replaced by their counterparts in L-ficolin. Mutations G221F and A256V inhibited binding to the 9-O-acetylated sialic acid derivatives, whereas Y271F abolished interaction with all sialic acid-containing glycans. The crystal structure of the Y271F mutant fibrinogen domain was solved, showing that the mutation does not alter the structure of the ligand binding pocket. These analyses reveal novel ficolin ligands such as sulfated N-acetyllactosamine (L-ficolin) and gangliosides (M-ficolin) and provide precise insights into the sialic acid binding specificity of M-ficolin, emphasizing the essential role of Tyr(271) in this respect.

Published
2009
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38. Molecular and functional characterization of the interaction of L-ficolin with Streptococcus pneumoniae

Author

Stermann, Emilie, Lacroix, Monique, Gout, Evelyne, Laffly, Emmanuelle, Pedersen, Christian Marcus, Schmidt, Richard R., Vernet, Thierry, Gaboriaud, Christine, Di Guilmi, Anne-Marie, Thielens, Nicole M., Stermann, Emilie, Lacroix, Monique, Gout, Evelyne, Laffly, Emmanuelle, Pedersen, Christian Marcus, Schmidt, Richard R., Vernet, Thierry, Gaboriaud, Christine, Di Guilmi, Anne-Marie, and Thielens, Nicole M.

Published
2012

45. Carbohydrate Recognition Properties of Human Ficolins

Author

Gout, Evelyne, primary, Garlatti, Virginie, additional, Smith, David F., additional, Lacroix, Monique, additional, Dumestre-Pérard, Chantal, additional, Lunardi, Thomas, additional, Martin, Lydie, additional, Cesbron, Jean-Yves, additional, Arlaud, Gérard J., additional, Gaboriaud, Christine, additional, and Thielens, Nicole M., additional

Published
2010
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