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Localization of nucleocapsid associated polypeptides in measles virus-infected cells by immunogold labelling after

W Bohn1, F Ciampor, R Rutter

  • 1Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie, Hamburg, Federal Republic of Germany.

Archives of Virology
|January 1, 1990
PubMed

Insights

Measles virus proteins localize to specific cellular sites, including nucleocapsids and the plasma membrane. Protein localization reveals distinct roles in virus assembly and budding, particularly for the matrix protein.

Area of Science:

  • Virology
  • Cell Biology

Background:

  • Measles virus is a significant human pathogen.
  • Understanding viral protein localization is crucial for comprehending its replication cycle.

Purpose of the Study:

  • To high-resolution localize measles virus nucleo-, phospho-, and matrix proteins within infected cells.
  • To elucidate the roles of these proteins in viral assembly and budding.

Main Methods:

  • Post-embedding immunogold labeling techniques were employed.
  • Monospecific and polyvalent antisera were used for high-resolution labeling.
  • Immunogold double labeling was performed to assess co-localization.

Main Results:

  • Viral proteins were non-randomly distributed, primarily in nucleocapsid inclusions and at the plasma membrane.
  • Phosphoprotein co-localized with nucleoprotein in cytoplasmic inclusions and budding virions, but not intranuclear inclusions.
  • Matrix protein was localized to assembled virus structures at the plasma membrane, with minimal cytoplasmic or intranuclear presence.

Conclusions:

  • Nucleocapsid composition varies depending on the cellular compartment.
  • This supports rapid assembly of paramyxovirus nucleocapsid polypeptides.
  • The matrix protein plays a selective role in measles virus assembly and plasma membrane budding.

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