Abstract
The antigenic epitopes of the myohemerythrin (MHr) molecule have been studied extensively. The critical amino acid residues responsible for its immune recognition have been identified by using synthetic peptides and the technique ofepitope scanning. To assess the true relevance of these techniques for determining the molecular mechanism of antigenic recognition and immunogenicity, the results obtained with isolated peptides should be tested in the context of the folded protein. To this end, we have designed and constructed a synthetic MHr gene, in modular form, which will allow subsequent alterations of nucleotide sequences encoding epitopes of interest. We have produced the recombinant protein at high level, and have shown by several criteria that it possesses the chemical, physical and immunological properties of the native worm protein. Thus, we have developed a valuable system for detailed immunological studies of the structure and chemistry required for antibody binding to protein.
Original language | English (US) |
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Pages (from-to) | 151-156 |
Number of pages | 6 |
Journal | Gene |
Volume | 99 |
Issue number | 2 |
DOIs | |
State | Published - Mar 15 1991 |
Externally published | Yes |
Keywords
- Recombinant DNA
- critical residues
- gene construction
- immune recognition
- protein antigenicity
- synthetic oligodeoxyribonucleotide
ASJC Scopus subject areas
- Genetics