title: Expression, purification and characterization of full-length RNA-free hepatitis B core particles.
abstract: The nucleocapsid or core particle of the hepatitis B virus has become one of the favourite recombinant vaccine carriers for foreign peptides, proteins and stimulatory oligonucleotides. The core protein consists of three regions: an N-terminal, a central and a C-terminal region that can accommodate the addition or insertion of the foreign sequences. The protamine-like C-terminal region that binds host RNA randomly during recombinant particle formation is often truncated. It is commonly thought that these truncations do not affect particle assembly. Recent studies have demonstrated that the C-terminal domains mediate a glycosaminoglycan-dependent attachment of nucleocapsids to the plasma membranes of host cells. This interaction might well contribute to the immunogenicity of nucleocapsids. Testing the hypothesis that full-length particles might be safer and superior for the induction of an immune response against the nucleocapsids and inserted sequences, requires the availability of purified particles. In this report, we detail a novel method for the synthesis and purification of full-length core particles essentially free of RNA from Escherichia coli.
authors: Laboratory of Plant Physiology, Department of Biology, 171 Groenenborgerlaan, Building U, 6th Floor, CGB University of Antwerp, 2020 Antwerpen, Belgium.
authors: Katleen
authors: K
authors: Broos
authors: Peter
authors: P
authors: Vanlandschoot
authors: Marleen
authors: M
authors: Maras
authors: Johan
authors: J
authors: Robbens
authors: Geert
authors: G
authors: Leroux-Roels
authors: Yves
authors: Y
authors: Guisez
mesh_terms: D001709:Biotechnology / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics; D006515:Hepatitis B virus / Q000276:immunology*; D019251:Nucleocapsid / Q000096:biosynthesis* / Q000302:isolation & purification / Q000648:ultrastructure; D012329:RNA, Bacterial / Q000032:analysis
chemical_list: D012329:RNA, Bacterial