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| Articles
by
Maria C de la Rosa |
Total Records (
1 ) for
Maria C de la Rosa |
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Nelson Acosta-Rivero
,
Joanna Poutou
,
Alexis Mussachio
,
Viviana Falcon
,
Yaraima Aguilera
,
Armando Rodriguez
,
Angel Perez
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Julio C. Aguilar
,
Maria C de la Rosa
,
Felix Alvarez
,
Juan Morales-Grillo
,
Juan Kouri
and
Santiago Duenas-Carrera
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Recently, it has been shown that HCV core proteins (HCcAg) with
C-terminal deletions assemble in vitro into virus-like particles (VLPs) in the
presence of structured RNA molecules. Results presented in this work showed
that a truncated HCcAg variant covering the first 120 aa (HCcAg.120) with a
32 aa N-terminal fusion peptide (6xHistag-XpressTMepitope) interacts with plasmid
DNA vaccine. Interestingly, the buoyant density of VLPs containing HCcAg.120
in CsCl gradients changed from 1.15-1,17 g mL1 to 1.30-1.34 g mL1 after addition
of plasmid DNA to assembly reactions. In addition, a delay in electrophoretic
mobility of HCcAg.120-plasmid samples on agarose gels was observed indicating
a direct interaction between VLPs and nucleic acids. Remarkably, addition of
either plasmid DNA or tRNA to assembly reactions leaded to heterogeneous and
larger VLPs formation than those observed in HCcAg.120 assembly reactions. VLPs
containing HCcAg.120 induced a specific IgG antibodies in mice that reacted
with hepatocytes from HCV-infected patients. VLPs obtained in this work would
be important to elucidate the mechanisms behind the ability of HCcAg to assemble
into a nucleocapsid structure. Besides, the capacity of particles containing
HCcAg.120 to interact with nucleic acids could be used in the development of
DNA vaccines and viral vectors based on these particles. |
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