| Literature DB >> 11779169 |
Nelson Acosta-Rivero1, Julio C Alvarez-Obregón, Alexis Musacchio, Viviana Falcón, Santiago Dueñas-Carrera, Jeny Marante, Ivón Menéndez, Juan Morales.
Abstract
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. (c)2002 Elsevier Science.Entities:
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Year: 2002 PMID: 11779169 DOI: 10.1006/bbrc.2001.6177
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575