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Successful mimicry of a complex viral antigen by multiple peptide insertions in a carrier protein
Author(s) -
Feliu Jordi X,
Carbonell Xavier,
Villaverde Antonio
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01582-9
Subject(s) - epitope , peptide , antigen , recombinant dna , antibody , molecular mimicry , virus , biology , virology , escherichia coli , peptide sequence , chemistry , microbiology and biotechnology , biochemistry , genetics , gene
The antigenic properties of a viral peptide from the surface of foot‐and‐mouth disease virus particles have been successfully mimicked by multiple insertion in solvent‐exposed regions of Escherichia coli β‐galactosidase. By increasing the number of viral peptides per enzyme monomer, the average IC 50 of hybrid proteins in a competitive enzyme‐linked immunosorbent assay) have decreased to values close to that presented by natural virions. Moreover, the antigenic diversity of these new recombinant enzymes when measured with different anti‐virus antibodies has also been largely reduced, indicating a better presentation of the epitopes located in the viral peptide. Although bivalent antibody binding could have been favoured by multiple presentation, conformational modifications of the viral peptide, due to the presence of other insertions or a cooperative antibody binding cannot be excluded. In addition, a multidimensional antigenic analysis have grouped together the multiple‐inserted proteins with the native virus, suggesting that increasing the number of insertions could be a good strategy to reproduce the antigenic properties of an immunoreactive peptide in a natural multimeric disposition.