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Analysis of the Solvent Accessibility of Cysteine Residues on Maize rayado fino virus Virus-like Particles Produced in Nicotiana benthamiana Plants and Cross-linking of Peptides to VLPs
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Maize rayado fino virus capsid proteins assemble into virus-like particles in Escherichia coli

Rosemarie W Hammond1, John Hammond

  • 1United States Department of Agriculture, Agricultural Research Service, Molecular Plant Pathology Laboratory, Plant Sciences Institute, Beltsville, MD 20705, USA. rose.hammond@ars.usda.gov

Virus Research
|November 17, 2009
PubMed

Insights

Maize rayado fino virus (MRFV) coat proteins CP1 and CP2 assemble into virus-like particles (VLPs) in E. coli. The N-terminal extension of CP1 is crucial for specific mRNA encapsidation.

Area of Science:

  • Plant virology
  • Molecular biology
  • Biochemistry

Background:

  • Maize rayado fino virus (MRFV) is a plant virus with two coat protein (CP) components, CP1 and CP2.
  • Both CP1 and CP2 are serologically related and form virus particles with a 3:1 molar ratio.
  • CP1 possesses a 37 amino acid N-terminal extension compared to CP2.

Purpose of the Study:

  • To investigate the role of MRFV coat proteins CP1 and CP2 in virus-like particle (VLP) assembly.
  • To determine the function of the N-terminal extension of CP1 in VLP formation and RNA encapsidation.
  • To understand the requirements for specific encapsidation of MRFV genomic RNA.

Main Methods:

  • Expression of individual CP1 and CP2 proteins in Escherichia coli.
  • Co-expression of CP1 and CP2 using a co-expression vector in E. coli.
  • Analysis of assembled VLPs using electron microscopy.
  • Determination of encapsidated RNA by molecular analysis.

Main Results:

  • Individual expression of CP1 or CP2 in E. coli resulted in the formation of VLPs.
  • CP1 VLPs were stain-impermeable and encapsidated bacterial 16S ribosomal RNA, but not CP mRNA.
  • CP2 VLPs were stain-permeable and did not encapsidate RNA.
  • Co-expression of CP1 and CP2 led to stain-impermeable VLPs that specifically encapsidated CP mRNA.

Conclusions:

  • The N-terminal 37 amino acid residues of CP1 are not essential for VLP assembly but may play a role in complete virion formation.
  • The presence of both CP1 and CP2 is necessary for the specific encapsidation of MRFV CP mRNA.
  • These findings provide insights into the mechanism of virion assembly and RNA packaging in Marafiviruses.

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