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Structural determinants of the interaction between influenza A virus matrix protein M1 and lipid membranes
Authors:C.T. Höfer  S. Di Lella  I. Dahmani  N. Jungnick  N. Bordag  S. Bobone  Q. Huang  S. Keller  A. Herrmann  S. Chiantia
Affiliation:1. Institute for Biology, IRI Life Sciences, Humboldt-Universität zu Berlin, Invalidenstraße 42, 10115, Berlin, Germany;2. University of Potsdam, Institute of Biochemistry and Biology, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany;3. Leibniz-Institute for Molecular Pharmacology (FMP), Biophysics of Membrane Proteins, Robert-Roessle-Str. 10, 13125 Berlin, Germany;4. School of Life Sciences, Fudan University, 220 Handan Rd, WuJiaoChang, Yangpu Qu, Shanghai Shi 200433, China;5. Molecular Biophysics, Technische Universität Kaiserslautern (TUK), Erwin-Schrödinger-Str. 13, 67663 Kaiserslautern, Germany
Abstract:Influenza A virus is a pathogen responsible for severe seasonal epidemics threatening human and animal populations every year. One of the ten major proteins encoded by the viral genome, the matrix protein M1, is abundantly produced in infected cells and plays a structural role in determining the morphology of the virus. During assembly of new viral particles, M1 is recruited to the host cell membrane where it associates with lipids and other viral proteins. The structure of M1 is only partially known. In particular, structural details of M1 interactions with the cellular plasma membrane as well as M1–protein interactions and multimerization have not been clarified, yet.In this work, we employed a set of complementary experimental and theoretical tools to tackle these issues. Using raster image correlation, surface plasmon resonance and circular dichroism spectroscopies, we quantified membrane association and oligomerization of full-length M1 and of different genetically engineered M1 constructs (i.e., N- and C-terminally truncated constructs and a mutant of the polybasic region, residues 95–105). Furthermore, we report novel information on structural changes in M1 occurring upon binding to membranes. Our experimental results are corroborated by an all-atom model of the full-length M1 protein bound to a negatively charged lipid bilayer.
Keywords:Corresponding authors.  Virus assembly  Protein-lipid interaction  Fluorescence microscopy  SPR  CD spectroscopy  Influenza A virus
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