tetano
Editor, Senior Moderator
Sci Rep. 2017 Jan 25;7:40801. doi: 10.1038/srep40801.
[h=1]The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.[/h] Saletti D[SUP]1,[/SUP][SUP]2[/SUP], Radzimanowski J[SUP]3[/SUP], Effantin G[SUP]3[/SUP], Midtvedt D[SUP]4[/SUP], Mangenot S[SUP]1,[/SUP][SUP]2[/SUP], Weissenhorn W[SUP]3[/SUP], Bassereau P[SUP]1,[/SUP][SUP]2[/SUP], Bally M[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 28120862 DOI: 10.1038/srep40801
[PubMed - in process] Free full text
[h=1]The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.[/h] Saletti D[SUP]1,[/SUP][SUP]2[/SUP], Radzimanowski J[SUP]3[/SUP], Effantin G[SUP]3[/SUP], Midtvedt D[SUP]4[/SUP], Mangenot S[SUP]1,[/SUP][SUP]2[/SUP], Weissenhorn W[SUP]3[/SUP], Bassereau P[SUP]1,[/SUP][SUP]2[/SUP], Bally M[SUP]1,[/SUP][SUP]2,[/SUP][SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 28120862 DOI: 10.1038/srep40801
[PubMed - in process] Free full text