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The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model

D. Saletti ; J. Radzimanowski ; G. Effantin ; Daniel Midtvedt (Institutionen för fysik, Biologisk fysik (Chalmers)) ; S. Mangenot ; W. Weissenhorn ; P. Bassereau ; Marta Bally (Institutionen för fysik, Biologisk fysik (Chalmers))
Scientific Reports (2045-2322). Vol. 7 (2017),
[Artikel, refereegranskad vetenskaplig]

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.



Denna post skapades 2017-02-17. Senast ändrad 2017-03-03.
CPL Pubid: 248206

 

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Institutioner (Chalmers)

Institutionen för fysik, Biologisk fysik (Chalmers)

Ämnesområden

Fysik

Chalmers infrastruktur