Abstract
AbstractThe core antigen of hepatitis B virus (HBcAg) made inEscherichia coliyields 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 multicomponent vaccines.
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
24 articles.
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