Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus
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-affi...
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Format: | Journal article |
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2014
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author | Leyrat, C Renner, M Harlos, K Huiskonen, J Grimes, J |
author_facet | Leyrat, C Renner, M Harlos, K Huiskonen, J Grimes, J |
author_sort | Leyrat, C |
collection | OXFORD |
description | 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. |
first_indexed | 2024-03-07T06:14:26Z |
format | Journal article |
id | oxford-uuid:f09a3774-8df2-4337-b1c2-0c4cb253e9bb |
institution | University of Oxford |
last_indexed | 2024-03-07T06:14:26Z |
publishDate | 2014 |
record_format | dspace |
spelling | oxford-uuid:f09a3774-8df2-4337-b1c2-0c4cb253e9bb2022-03-27T11:49:22ZStructure and self-assembly of the calcium binding matrix protein of human metapneumovirusJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f09a3774-8df2-4337-b1c2-0c4cb253e9bbSymplectic Elements at Oxford2014Leyrat, CRenner, MHarlos, KHuiskonen, JGrimes, JThe 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. |
spellingShingle | Leyrat, C Renner, M Harlos, K Huiskonen, J Grimes, J Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title_full | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title_fullStr | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title_full_unstemmed | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title_short | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus |
title_sort | structure and self assembly of the calcium binding matrix protein of human metapneumovirus |
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