National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM114561
米国
National Science Foundation (NSF, United States)
0923395
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R21AI101775
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
R01HD079327
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R01AI083402
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
F32GM112517
米国
引用
ジャーナル: Nat Commun / 年: 2018 タイトル: Promotion of virus assembly and organization by the measles virus matrix protein. 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 / 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.