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Replication of alfamo- and ilarviruses: role of the coat protein

John F Bol1

  • 1Institute of Biology, Gorlaeus Laboratories, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands. j.bol@chem.leidenuniv.nl

Annual Review of Phytopathology
|August 5, 2005
PubMed

Insights

Alfalfa mosaic virus (AMV) coat protein (CP) binding to viral RNA enhances translation and blocks RNA synthesis. This CP binding is proposed to initiate infection by mimicking poly(A)-binding protein functions.

Area of Science:

  • Plant Virology
  • Molecular Biology
  • RNA Biology

Background:

  • Bromoviridae family viruses exhibit varied infectivity based on genomic RNA and coat protein (CP) requirements.
  • Alfalfa mosaic virus (AMV), an alfamovirus, requires CP binding to its 3' end for infection initiation.
  • The 3' end of AMV RNAs can form distinct structures influencing viral processes.

Purpose of the Study:

  • To investigate the early functions of Alfalfa mosaic virus (AMV) coat protein (CP).
  • To elucidate the mechanism by which CP binding initiates viral infection.
  • To understand the impact of CP binding on viral RNA translation and replication.

Main Methods:

  • Analysis of Alfalfa mosaic virus (AMV) RNA 3' end conformations.
  • In vitro and in vivo studies on the effects of CP binding to viral RNA.
  • Comparative analysis of viral RNA structures and CP binding sites.

Main Results:

  • AMV RNA's 3' end adopts two conformations: one with tRNA-like structure for minus-strand promoter activity, and another with hairpins for CP binding.
  • CP binding significantly enhances viral RNA translational efficiency (40-fold in vivo).
  • CP binding inhibits viral minus-strand RNA synthesis in vitro.

Conclusions:

  • AMV CP plays a dual role in infection initiation and regulation of viral RNA metabolism.
  • CP binding to the 3' end of AMV RNA is crucial for efficient translation.
  • AMV CP is hypothesized to initiate infection by mimicking cellular poly(A)-binding protein functions.

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