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1. Mechanical Control of Cell Migration by the Metastasis Suppressor Tetraspanin CD82/KAI1

Author

Laura Ordas, Luca Costa, Anthony Lozano, Christopher Chevillard, Alexia Calovoulos, Diala Kantar, Laurent Fernandez, Lucie Chauvin, Patrice Dosset, Christine Doucet, Lisa Heron-Milhavet, Elena Odintsova, Fedor Berditchevski, Pierre-Emmanuel Milhiet, and Christine Bénistant

Subjects
cell migration, plasma membrane, tetraspanins, caveolins, focal adhesions, actin, Cytology, QH573-671
Abstract

The plasma membrane is a key actor of cell migration. For instance, its tension controls persistent cell migration and cell surface caveolae integrity. Then, caveolae constituents such as caveolin-1 can initiate a mechanotransduction loop that involves actin- and focal adhesion-dependent control of the mechanosensor YAP to finely tune cell migration. Tetraspanin CD82 (also named KAI-1) is an integral membrane protein and a metastasis suppressor. Its expression is lost in many cancers including breast cancer. It is a strong inhibitor of cell migration by a little-known mechanism. We demonstrated here that CD82 controls persistent 2D migration of EGF-induced single cells, stress fibers and focal adhesion sizes and dynamics. Mechanistically, we found that CD82 regulates membrane tension, cell surface caveolae abundance and YAP nuclear translocation in a caveolin-1-dependent manner. Altogether, our data show that CD82 controls 2D cell migration using membrane-driven mechanics involving caveolin and the YAP pathway.

Published
2021
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2. Elicitation of potent SARS-CoV-2 neutralizing antibody responses through immunization using a versatile adenovirus-inspired multimerization platform

Author

Isabelle Bally, Pascal Fender, Daphna Fenel, Evelyne Gout, Solene Besson, Christopher Chevillard, M. Buisson, Axelle Amen, Dalil Hannani, Guy Schoehn, Christophe Moreau, Pascal Poignard, Salome Gallet, Marie-Claire Dagher, Valentin Dettling, Emilie Vassal-Stermann, 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), Translational microbial Evolution and Engineering (TIMC-TrEE), Translational Innovation in Medicine and Complexity / Recherche Translationnelle et Innovation en Médecine et Complexité - UMR 5525 (TIMC ), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Université Grenoble Alpes (UGA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Université Grenoble Alpes (UGA), GEFLUC Dauphiné-Savoie, Ligue contre le Cancer Comité Isère, Université Grenoble, Alpes IDEX Initiatives de Recherche Stratégiques and Fondation du Souffle-Fonds de recherche en santé respiratoire (FdS-FRSR), Région Auvergne Rhône-Alpes, AuRA, MEM, ISBG, and ANR-20-COVI-0000,Flash Covid Cov Mime

Subjects
Infectivity, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, viruses, [SDV]Life Sciences [q-bio], biochemical phenomena, metabolism, and nutrition, Virology, Neutralization, 3. Good health, Herd immunity, 03 medical and health sciences, Titer, 0302 clinical medicine, Antigen, Immunization, Immunity, biology.protein, Neutralizing antibody, 030217 neurology & neurosurgery, 030304 developmental biology
Abstract

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic has shown that vaccine preparedness is critical to anticipate a fast response to emergent pathogens with high infectivity. To rapidly reach herd immunity, an affordable, easy to store and versatile vaccine platform is thus desirable. We previously designed a non-infectious adenovirus-inspired nanoparticle (ADDomer), and in the present work, we efficiently decorated this original vaccine platform with glycosylated receptor binding domain (RBD) of SARS-CoV-2. Cryo-Electron Microscopy structure revealed that up to 60 copies of this antigenic domain were bound on a single ADDomer particle with the symmetrical arrangements of a dodecahedron. Mouse immunization with the RBD decorated particles showed as early as the first immunization a significant anti-coronavirus humoral response, which was boosted after a second immunization. Neutralization assays with spike pseudo-typed-virus demonstrated the elicitation of strong neutralization titers. Remarkably, the existence of pre-existing immunity against adenoviral-derived particles enhanced the humoral response against SARS-CoV-2. This plug and play vaccine platform revisits the way of using adenovirus to combat emergent pathogens while potentially taking advantage of the adenovirus pre-immunity.

Published
2021

3. Mechanical Control of Cell Migration by the Metastasis Suppressor Tetraspanin CD82/KAI1

Author

Diala Kantar, Luca Costa, Fedor Berditchevski, Laurent Fernandez, Lucie Chauvin, Christopher Chevillard, Elena Odintsova, Laura Ordas, Patrice Dosset, Lisa Heron-Milhavet, Anthony Lozano, Alexia Calovoulos, Christine Benistant, Christine Doucet, Pierre-Emmanuel Milhiet, Centre de Biochimie Structurale [Montpellier] (CBS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), 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), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Acides Nucléiques : Régulations Naturelle et Artificielle (ARNA), Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institute of Cancer and Genomic Sciences, University of Birmingham, Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), and Milhiet, Pierre-Emmanuel

Subjects
cell migration, QH301-705.5, Cell, Caveolin 1, [SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, [SDV.CAN]Life Sciences [q-bio]/Cancer, Kangai-1 Protein, plasma membrane, Mechanotransduction, Cellular, Article, Cell Line, Focal adhesion, 03 medical and health sciences, 0302 clinical medicine, [SDV.CAN] Life Sciences [q-bio]/Cancer, Tetraspanin, Cell Movement, Caveolae, Cell Line, Tumor, Neoplasms, Stress Fibers, Caveolin, medicine, Cell Adhesion, Humans, Biology (General), Mechanotransduction, Neoplasm Metastasis, 030304 developmental biology, caveolins, mechanotransduction, 0303 health sciences, Chemistry, Cell Membrane, Membrane Proteins, Cell migration, General Medicine, focal adhesions, Cell biology, tetraspanins, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, medicine.anatomical_structure, 030220 oncology & carcinogenesis, YAP, CD82, actin, Signal Transduction, Transcription Factors
Abstract

International audience; The plasma membrane is a key actor of cell migration. For instance, its tension controls persistent cell migration and cell surface caveolae integrity. Then, caveolae constituents such as caveolin-1 can initiate a mechanotransduction loop that involves actin- and focal adhesion-dependent control of the mechanosensor YAP to finely tune cell migration. Tetraspanin CD82 (also named KAI-1) is an integral membrane protein and a metastasis suppressor. Its expression is lost in many cancers including breast cancer. It is a strong inhibitor of cell migration by a little-known mechanism. We demonstrated here that CD82 controls persistent 2D migration of EGF-induced single cells, stress fibers and focal adhesion sizes and dynamics. Mechanistically, we found that CD82 regulates membrane tension, cell surface caveolae abundance and YAP nuclear translocation in a caveolin-1-dependent manner. Altogether, our data show that CD82 controls 2D cell migration using membrane-driven mechanics involving caveolin and the YAP pathway.

Published
2021
Full Text
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4. Mechanical Control of Cell Migration by the Metastasis Suppressor Tetraspanin CD82/KAI1

Author

Fedor Berditchevski, Lucie Chauvin, Elena Odinstova, Alexia Calovoulos, Anthony Lozano, Christopher Chevillard, Laura Ordas, Pierre-Emmanuel Milhiet, Christine Doucet, Eric Rubinstein, Luca Costa, Laurent Fernandez, Christine Benistant, and Patrice Dosset

Subjects
Focal adhesion, medicine.anatomical_structure, Tetraspanin, Chemistry, Caveolae, Cell, Caveolin, medicine, Metastasis suppressor, Cell migration, CD82, Cell biology
Abstract

The plasma membrane is a key actor of cell migration. For instance, its tension controls persistent cell migration and cell surface caveolae integrity. Then, caveolae constituents like caveolin-1 can initiate a mechano-tranduction loop that involves actin-and focal adhesions- dependent control of the mechanosensor YAP to finely tune cell migration. Tetraspanin CD82 (also named KAI-1) is an integral membrane protein and a metastasis suppressor. Its expression is lost in many cancers including breast cancer. It is a strong inhibitor of cell migration by a not well-known mechanism. We demonstrated here that CD82 controls persistent 2D migration of EGF-induced single cell, stress fibers and focal adhesion sizes and dynamics. In addition, CD82 regulates cell mechanics e.g. membrane tension, cell surface caveolae abundance and YAP nuclear translocation in a caveolin-1 dependent manner. Altogether, our data strongly suggest that CD82 controls 2D cell migration using a membrane-driven mechanical loop involving caveolin and the YAP pathway.

Published
2020
Full Text
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