The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model
Artikel i vetenskaplig tidskrift, 2017

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.

Författare

D. Saletti

Physico-Chimie Curie

Sorbonne Université

J. Radzimanowski

Université Grenoble Alpes

G. Effantin

Université Grenoble Alpes

Daniel Midtvedt

Chalmers, Fysik, Biologisk fysik

S. Mangenot

Physico-Chimie Curie

Sorbonne Université

W. Weissenhorn

Université Grenoble Alpes

P. Bassereau

Physico-Chimie Curie

Sorbonne Université

Marta Bally

Chalmers, Fysik, Biologisk fysik

Scientific Reports

2045-2322 (ISSN)

Vol. 7 40801

Ämneskategorier

Fysik

DOI

10.1038/srep40801

Mer information

Skapat

2017-10-07