In vitro self-assembled HCV core virus-like particles induce a strong antibody immune response in sheep.
The in vitro self-assembly properties of the entire hepatitis C virus core protein (HCcAg) obtained from Pichia pastoris cells and the induction of specific antibody immune response were studied. HCcAg was purified as a low-molecular-weight species by electroelution under denaturing conditions for confirmation of its self-assembly properties. After renaturalization, electron microscopy showed that HCcAg assembled into spherical particles of 30 nm. HCcAg also showed homogeneity and was specifically recognized by serum from a chronic HCV carrier patient. The data indicated that in vitro assembly of HCcAg, into virus-like particles resembling HCV nucleocapsid particles at a mature stage, is an intrinsic quality of this protein. Finally, HCcAg generated a strong antibody immune response in sheep, suggesting its usefulness for stimulating the host immune response against HCV.
Acosta-Rivero
Nelson
N
Division of Vaccines, Center for Genetic Engineering and Biotechnology, Ave. 31 e/158 y 190, P.O. Box 61562, C.P. 10 600, Havana City, Cuba. nelson.acosta@cigb.edu.cu
Alvarez-Obregón
Julio C
JC
Musacchio
Alexis
A
Falcón
Viviana
V
Dueñas-Carrera
Santiago
S
Marante
Jeny
J
Menéndez
Ivón
I
Morales
Juan
J
D000818:Animals; D000956:Antigens, Viral / Q000302:isolation & purification; D000998:Antiviral Agents / Q000494:pharmacology; D015153:Blotting, Western; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D016174:Hepacivirus / Q000737:chemistry*; D006505:Hepatitis / Q000188:drug therapy; D006801:Humans; D015151:Immunoblotting; D051379:Mice; D008854:Microscopy, Electron; D019590:Nucleocapsid Proteins / Q000737:chemistry / Q000648:ultrastructure; D010843:Pichia / Q000378:metabolism; D013997:Time Factors; D014758:Viral Core Proteins / Q000737:chemistry*
D000956:Antigens, Viral; D000998:Antiviral Agents; D019590:Nucleocapsid Proteins; D014758:Viral Core Proteins