Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus.
作者： Cedric Leyrat , Max Renner , Karl Harlos , Juha T. Huiskonen , Jonathan M. Grimes
DOI: 10.1016/J.STR.2013.10.013
关键词: VP40 、 Viral matrix protein 、 Binding site 、 Biology 、 Human metapneumovirus 、 Crystallography 、 Crystal structure 、 Calcium-binding protein 、 Metapneumovirus 、 Molecular dynamics
摘要: 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 human metapneumovirus M at 2.8 A resolution its native dimeric state. reveals presence high-affinity Ca2+ binding site. Molecular dynamics simulations (MDS) predict secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering MDS ensemble analysis, captured solution. Our analysis large positively charged patch on surface is involved membrane interaction. Structural DOPC-induced polymerization into helical filaments using electron microscopy leads to model self-assembly. conservation sites suggests for calcium replication morphogenesis pneumoviruses.
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