Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus

Journal article

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 Ca 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 Ca binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses. © 2014 Elsevier Ltd All rights reserved.

Authors: Leyrat, C; Renner, M; Harlos, K; Huiskonen, J; Grimes, J

• Journal: Structure
• Volume: 22
• Issue: 1
• Pages: 136-148
• Publication date: 2014-01-07
• DOI: 10.1016/j.str.2013.10.013
• EISSN: 1878-4186
• ISSN: 0969-2126