Abstract
The core antigen of hepatitis B virus (HBcAg) made in Escherichia coli yields particles that closely resemble the viral nucleocapsid. Extensive modifications can be made to the primary structure of HBcAg without impairing particle assembly. This enables other peptide sequences, including very long sequences, to be added, substituted, or inserted into the nucleocapsid subunit while retaining the ability to form highly immunogenic particles. These also retain the T cell epitopes of HBcAg and constitute powerful delivery systems for a diverse range of immunogenic epitopes and have significant potential for development of multi-component vaccines.
Original language | English |
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Pages (from-to) | 277-283 |
Number of pages | 7 |
Journal | Biological Chemistry |
Volume | 380 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1999 Mar |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Clinical Biochemistry