Journal of General Virology, Vol 78, 2049-2053, Copyright © 1997 by Society for General Microbiology

ARTICLES

Mosaic hepatitis B virus core particles allow insertion of extended foreign protein segments

D Koletzki, A Zankl, HR Gelderblom, H Meisel, A Dislers, G Borisova, P Pumpens, DH Kruger and R Ulrich
Institute of Medical Virology, Charite, Humboldt-University, Berlin, Germany.

Because of its particular immunological properties, the core protein of hepatitis B virus (HBcAg) has become one of the favoured 'virus-like particles' for use as a carrier of foreign epitopes. A new strategy to construct core particles presenting extended foreign protein segments was established based on the introduction of a linker containing a translational stop codon between sequences encoding a C-terminally truncated HBcAg (HBcAg delta) and a foreign protein sequence. Expression in an Escherichia coli suppressor strain allowed the simultaneous synthesis of both HBcAg delta and a read-through fusion protein containing a part of the hantavirus nucleocapsid protein. After purification, the presence of core-like mosaic particles with HBc and hantavirus antigenicity was demonstrated by electron microscopy and immunological tests. This strategy of partial stop codon suppression should improve the use of HBcAg as a carrier of foreign epitopes by allowing insertion of long foreign sequences into particle-forming proteins. The resulting mosaic particles should be of general interest for further vaccine developments.

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