Analysis of foreign epitope inserts in HBcAg. Approaches to solving the problem of core particle self-assembly

Autor: Karpenko, L. I., Ivanisenko, V. A., Pika, I. S., Chikaev, N. A., Eroshkin, A. M., Melamed, N. V., Veremeiko, T. A., Il’ichev, A. A.
Zdroj: Molecular Biology; March 2000, Vol. 34 Issue: 2 p194-199, 6p
Abstrakt: The hepatitis B virus core antigen (HBcAg) is a promising protein carrier for exposing the epitopes of various human and animal pathogens. HBcAg-based chimeric proteins can be used in creating highly efficient vaccines; however, not all chimeric HBcAg with foreign epitope inserts are capable of assembly into virus-like particles. Using computer programs ProAnalyst, SALIX, and QSARPro, we examined the relationship between the self-assembly capability of chimeric HBcAg and the physicochemical properties of the inserts. The self-assembly was found to be impaired when the inserted peptides contained highly hydrophobic and bulky residues tending to form β-structures; this especially concerned the C-proximal residues in the insert. Recommendations were elaborated for constructing foreign epitopes that would ensure correct self-assembly of chimeric HBcAg particles.
Databáze: Supplemental Index
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