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The matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 Å resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca²⁺ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca²⁺ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses.

Original publication

DOI

10.1016/j.str.2013.10.013

Type

Journal article

Journal

Structure

Publication Date

07/01/2014

Volume

22

Pages

136 - 148

Keywords

Calcium, Calcium-Binding Proteins, Escherichia coli, Humans, Metapneumovirus, Microscopy, Electron, Molecular Dynamics Simulation, Phosphatidylcholines, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Scattering, Small Angle, Thermodynamics, Viral Matrix Proteins, Virion, Virus Assembly, Virus Replication, X-Ray Diffraction