title: The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.
abstract: Matrix proteins from enveloped viruses play an important role in budding and stabilizing virus particles. In order to assess the role of the matrix protein M1 from influenza C virus (M1-C) in plasma membrane deformation, we have combined structural and in vitro reconstitution experiments with model membranes. We present the crystal structure of the N-terminal domain of M1-C and show by Small Angle X-Ray Scattering analysis that full-length M1-C folds into an elongated structure that associates laterally into ring-like or filamentous polymers. Using negatively charged giant unilamellar vesicles (GUVs), we demonstrate that M1-C full-length binds to and induces inward budding of membrane tubules with diameters that resemble the diameter of viruses. Membrane tubule formation requires the C-terminal domain of M1-C, corroborating its essential role for M1-C polymerization. Our results indicate that M1-C assembly on membranes constitutes the driving force for budding and suggest that M1-C plays a key role in facilitating viral egress.
authors.affiliation: Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.|Sorbonne Universités, UPMC Univ Paris 06, 75005, Paris, France.
authors.forename: David
authors.initials: D
authors.lastname: Saletti
authors.affiliation: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000 Grenoble, France.
authors.forename: Jens
authors.initials: J
authors.lastname: Radzimanowski
authors.affiliation: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000 Grenoble, France.
authors.forename: Gregory
authors.initials: G
authors.lastname: Effantin
authors.affiliation: Department of Physics, Chalmers University of Technology, Gothenburg, Sweden.
authors.forename: Daniel
authors.initials: D
authors.lastname: Midtvedt
authors.affiliation: Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.|Sorbonne Universités, UPMC Univ Paris 06, 75005, Paris, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Mangenot
authors.affiliation: Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000 Grenoble, France.
authors.forename: Winfried
authors.initials: W
authors.lastname: Weissenhorn
authors.affiliation: Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.|Sorbonne Universités, UPMC Univ Paris 06, 75005, Paris, France.
authors.forename: Patricia
authors.initials: P
authors.lastname: Bassereau
authors.affiliation: Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.|Sorbonne Universités, UPMC Univ Paris 06, 75005, Paris, France.|Department of Physics, Chalmers University of Technology, Gothenburg, Sweden.
authors.forename: Marta
authors.initials: M
authors.lastname: Bally
mesh_terms: D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism* / Q000821:virology*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D009982:Gammainfluenzavirus / Q000502:physiology*; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D011994:Recombinant Proteins; D055672:Static Electricity; D013329:Structure-Activity Relationship; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D014763:Viral Matrix Proteins