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-Structure paper
タイトル | Structure and assembly of a paramyxovirus matrix protein. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 109, Issue 35, Page 13996-14000, Year 2012 |
掲載日 | 2012年8月28日 |
著者 | Anthony J Battisti / Geng Meng / Dennis C Winkler / Lori W McGinnes / Pavel Plevka / Alasdair C Steven / Trudy G Morrison / Michael G Rossmann / |
PubMed 要旨 | Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and ...Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and cryoelectron tomography to show that the matrix protein of Newcastle disease virus, a paramyxovirus and relative of measles virus, forms dimers that assemble into pseudotetrameric arrays that generate the membrane curvature necessary for virus budding. We show that the glycoproteins are anchored in the gaps between the matrix proteins and that the helical nucleocapsids are associated in register with the matrix arrays. About 90% of virions lack matrix arrays, suggesting that, in agreement with previous biological observations, the matrix protein needs to dissociate from the viral membrane during maturation, as is required for fusion and release of the nucleocapsid into the host's cytoplasm. Structure and sequence conservation imply that other paramyxovirus matrix proteins function similarly. |
リンク | Proc Natl Acad Sci U S A / PubMed:22891297 / PubMed Central |
手法 | EM (サブトモグラム平均) / X線回折 |
解像度 | 2.2 - 45.6 Å |
構造データ | EMDB-5448: PDB-4g1g: PDB-4g1l: PDB-4g1o: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / Beta strand / Virus assembly / Membrane / Virus / Beta-strand / matrix protein / Viurs |