Abstract
The oligomeric recombinant protein DB-1 containing the immunodominant sites of the circumsporozoite protein of Plasmodium falciparum and tetanus toxin was constructed to optimize the schemes of presentation of B-cell epitopes during vaccination with chimeric proteins without the use of adjuvants. A fragment of the pentameric coiled-coil human cartilage oligomeric matrix protein was used as an oligomerization matrix. The expression of the protein in Escherichia coli cells was studied, a method for its purification was developed, and it was biochemically characterized.
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Belitskaya, S.Y., Boldyreva, E.F. & Korobko, V.G. Design of Chimeric Proteins on the Basis of a Pentameric Superhelical Fragment of Human Cartilage Oligomeric Matrix Protein: I. The Properties of a Hybrid Containing the Immunodominant Domain of the Circumsporozoite Protein of Plasmodium falciparum . Russian Journal of Bioorganic Chemistry 30, 35–41 (2004). https://doi.org/10.1023/B:RUBI.0000015771.70401.d3
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DOI: https://doi.org/10.1023/B:RUBI.0000015771.70401.d3