Assembly of truncated HCV core antigen into virus-like particles in Escherichia coli.
Core protein is one of the most conserved and immunogenic of the hepatitis C virus proteins. Several pieces of experimental evidence suggest its ability for formation of virus like particles alone or in association with other viral proteins in mammalian or yeast cells with great similarity to those detected in patient sera and liver extract. In this work we report an Escherichia coli-derived truncated hepatitis C core protein that is able to aggregate. SDS-PAGE and size exclusion chromatography patterns bring to mind the aggregation of monomers of recombinant protein Co.120. The Co.120 protein migrated with buoyant density of 1.28 g/cm(3) when analyzed using CsCl density gradient centrifugation. Spherical structures with an average diameter of 30 nm were observed using electron microscopy. We report here that VLPs are generated when the first 120 aa of HCV core protein are expressed in E. coli.
Vaccine Department, HCV Section, Center for Genetic Engineering and Biotechnology, Havana City, Cuba.
L J
LJ
Lorenzo
S
S
Dueñas-Carrera
V
V
Falcón
N
N
Acosta-Rivero
E
E
González
M C
MC
de la Rosa
I
I
Menéndez
J
J
Morales
D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000821:virology*; D016174:Hepacivirus / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D018936:Hepatitis C Antigens / Q000378:metabolism / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D014758:Viral Core Proteins / Q000378:metabolism* / Q000648:ultrastructure
D018936:Hepatitis C Antigens; D014758:Viral Core Proteins; C069130:nucleocapsid protein, Hepatitis C virus