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Murine leukemia virus transmembrane protein R-peptide is found in small virus core-like complexes in cells

Klaus Bahl Andersen1, Huong Ai Diep1, Anne Zedeler1

  • 1Department of Pharmacology and Pharmacotherapy, The Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark.

The Journal of General Virology
|May 13, 2006
PubMed

Insights

The R-peptide from the Murine leukemia virus (MLV) envelope protein binds to core particles before budding. This interaction facilitates the virus acquiring envelope proteins during assembly.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Murine leukemia virus (MLV) assembly involves Gag protein, viral RNA, and cell membrane proteins.
  • Viral envelope proteins are acquired during the budding process, but the mechanism remains unclear.

Purpose of the Study:

  • To elucidate the mechanism by which Murine leukemia virus (MLV) acquires envelope proteins during assembly.
  • To investigate the role of the R-peptide in the association of envelope proteins with viral core particles.

Main Methods:

  • Analysis of Moloney MLV particles and infected cells.
  • Characterization of Gag-containing complexes using density gradient centrifugation and size analysis.

Main Results:

  • R-peptide was found to bind to MLV core particles.
  • R-peptide and uncleaved TM associate with small, core-like complexes in cells.
  • These complexes are mild detergent-insoluble, Gag-containing, with a density of 1.23 g/ml and size of 150-200 S.

Conclusions:

  • The R-peptide mediates the association of the TM protein with the assembling viral core particle prior to budding.
  • This R-peptide-mediated interaction is the mechanism by which budding MLV acquires its envelope proteins.

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