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-Structure paper
タイトル | Promotion of virus assembly and organization by the measles virus matrix protein. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 1736, Year 2018 |
掲載日 | 2018年4月30日 |
著者 | Zunlong Ke / Joshua D Strauss / Cheri M Hampton / Melinda A Brindley / Rebecca S Dillard / Fredrick Leon / Kristen M Lamb / Richard K Plemper / Elizabeth R Wright / |
PubMed 要旨 | Measles virus (MeV) remains a major human pathogen, but there are presently no licensed antivirals to treat MeV or other paramyxoviruses. Here, we use cryo-electron tomography (cryo-ET) to elucidate ...Measles virus (MeV) remains a major human pathogen, but there are presently no licensed antivirals to treat MeV or other paramyxoviruses. Here, we use cryo-electron tomography (cryo-ET) to elucidate the principles governing paramyxovirus assembly in MeV-infected human cells. The three-dimensional (3D) arrangement of the MeV structural proteins including the surface glycoproteins (F and H), matrix protein (M), and the ribonucleoprotein complex (RNP) are characterized at stages of virus assembly and budding, and in released virus particles. The M protein is observed as an organized two-dimensional (2D) paracrystalline array associated with the membrane. A two-layered F-M lattice is revealed suggesting that interactions between F and M may coordinate processes essential for MeV assembly. The RNP complex remains associated with and in close proximity to the M lattice. In this model, the M lattice facilitates the well-ordered incorporation and concentration of the surface glycoproteins and the RNP at sites of virus assembly. |
リンク | Nat Commun / PubMed:29712906 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 20.0 - 50.0 Å |
構造データ | EMDB-7565: EMDB-7566: EMDB-7587: EMDB-7588: EMDB-7590: EMDB-7591: EMDB-7594: EMDB-7595: EMDB-7596: EMDB-7597: |