A C-terminal truncated hepatitis C virus core protein variant assembles in vitro into virus-like particles in the absence of structured nucleic acids.

@article{AcostaRivero2005ACT,
  title={A C-terminal truncated hepatitis C virus core protein variant assembles in vitro into virus-like particles in the absence of structured nucleic acids.},
  author={Nelson Acosta-Rivero and Armando L. Rodriguez and Alexis Mussachio and Johana Poutou and Viviana Falc{\'o}n and Dinorah R Torres and Julio C. Aguilar and Marbelis Linares and Mabel Alonso and Angel Palacios P{\'e}rez and Iv{\'o}n Men{\'e}ndez and Juan Morales-Grillo and Gabriel M{\'a}rquez and Santiago Due{\~n}as-Carrera},
  journal={Biochemical and biophysical research communications},
  year={2005},
  volume={334 3},
  pages={901-6}
}
Little is known about the assembly pathway or structure of the hepatitis C virus (HCV). In this work a truncated HCcAg variant covering the first 120 aa (HCcAg.120) with a 32 aa N-terminal fusion peptide (6x Histag-Xpress epitope) was purified as a monomer under strong denaturing conditions. In addition, minor HCcAg.120 peaks exhibiting little different molecular mass by SDS-PAGE which possibly represents alternative forms harboring the N-termini of HCcAg.120 were detected. Analysis using gel… CONTINUE READING

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