Year: 2013
Type: article
Abstract: 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.
Source: Structure
Language: English
Topic: Virology and Viral Diseases
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $4,851
Awards: e-Infrastructure South Consortium - Centre for Innovation, e-Infrastructure South Consortium - Centre for Innovation, G6943782598, Understanding the genetic basis of common human diseases: core funding for the Wellcome Trust Centre for Human Genetics., Purchase of electron microscopic infrastructure to establish a multi-user facility for cryo electron microscopy, in particular cryo electron tomography., G7556047725
OpenAlex ID: W2005209853