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Promotion of virus assembly and organization by the measles virus matrix protein

Zunlong Ke1,2, Joshua D Strauss1, Cheri M Hampton1

  • 1Division of Infectious Diseases, Department of Pediatrics, Emory University School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA, 30322, USA.

Nature Communications
|May 2, 2018
PubMed

Insights

Measles virus assembly involves a matrix protein lattice coordinating surface glycoproteins and ribonucleoprotein complexes. This finding offers insights for developing new paramyxovirus antivirals.

Area of Science:

  • Virology
  • Structural Biology
  • Cell Biology

Background:

  • Measles virus (MeV) is a significant human pathogen with no current antiviral treatments.
  • Understanding paramyxovirus assembly is crucial for therapeutic development.

Purpose of the Study:

  • To elucidate the principles of MeV assembly using cryo-electron tomography (cryo-ET).
  • To characterize the 3D arrangement of MeV structural proteins during assembly.

Main Methods:

  • Cryo-electron tomography (cryo-ET) was employed to visualize MeV assembly in infected human cells.
  • Detailed analysis of the spatial organization of matrix (M) protein, surface glycoproteins (F and H), and ribonucleoprotein (RNP) complexes.

Main Results:

  • The M protein forms a 2D paracrystalline array at the cell membrane during assembly.
  • A two-layered F-M lattice structure was identified, suggesting coordination between F and M proteins.
  • The RNP complex remains closely associated with the M protein lattice.

Conclusions:

  • The M protein lattice is central to MeV assembly, organizing glycoproteins and RNP complexes.
  • These findings provide a structural basis for understanding paramyxovirus assembly.
  • The study offers potential targets for novel antiviral strategies against measles and other paramyxoviruses.

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