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Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic

Valera V Peremyslov1, Yung-Wei Pan, Valerian V Dolja

  • 1Department of Botany and Plant Pathology and Center for Gene Research and Biotechnology, Oregon State University, Corvallis, Oregon 97331, USA.

Journal of Virology
|March 16, 2004
PubMed

Insights

Beet yellows virus movement protein p6 associates with the endoplasmic reticulum. Its domains and dimerization are crucial for cell-to-cell transport of the virus.

Area of Science:

  • Plant Virology
  • Molecular Plant Pathology
  • Cell Biology

Background:

  • Cell-to-cell movement of Beet yellows closterovirus (BYV) is essential for its systemic infection.
  • This movement relies on four structural proteins and a nonstructural 6-kDa protein (p6), identified as the viral movement protein.

Purpose of the Study:

  • To investigate the subcellular localization and functional domains of the p6 movement protein.
  • To elucidate the molecular mechanisms underlying p6-mediated viral transport in infected plants.

Main Methods:

  • Localization studies via virus infection and p6 overexpression.
  • Analysis of p6 protein structure, including transmembrane domains and disulfide bridge formation.
  • Mutagenic analysis to assess the role of p6 domains and dimerization in viral movement.

Main Results:

  • Virus infection or p6 overexpression leads to p6 association with the rough endoplasmic reticulum (RER).
  • p6 features a single-span transmembrane N-terminal domain and a cytoplasmic C-terminal domain.
  • p6 forms a disulfide bridge in infected cells, and both its domains and dimerization are vital for function.

Conclusions:

  • The p6 movement protein localizes to the endoplasmic reticulum, suggesting a role in ER-mediated transport.
  • Specific structural features of p6, including its domains and ability to dimerize, are critical for its role in facilitating BYV cell-to-cell movement.

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