Open AccessNewly Characterized Species-Specific ImmunogenicChlamydophila pneumoniaePeptide Reactive with Murine Monoclonal and Human Serum Antibodies
Author(s) -
Eric L. Marston,
Andrea V. James,
Jake Parker,
John Hart,
Teresa M. Brown,
Trudy O. Messmer,
Danny L. Jue,
Carolyn M. Black,
George M. Carlone,
Edwin W. Ades,
Jacquelyn S. Sampson
Publication year - 2002
Publication title -
clinical and vaccine immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.649
H-Index - 77
eISSN - 1556-6811
pISSN - 1556-679X
DOI - 10.1128/cdli.9.2.446-452.2002
Subject(s) - mimotope , monoclonal antibody , epitope , chlamydophila pneumoniae , phage display , chlamydophila , biology , peptide , antibody , paratope , microbiology and biotechnology , peptide library , virology , peptide vaccine , chlamydia trachomatis , chlamydiaceae , peptide sequence , biochemistry , chlamydia , immunology , gene
A monoclonal antibody (MAb) directed against an unknown Chlamydophila pneumoniae epitope has been characterized, and the respective peptide mimotope has been identified. A murine MAb specific for C. pneumoniae was used to select peptides from phage display libraries. The peptides identified from the phage display library clones reacted specifically with the respective target murine MAb and with human sera previously identified as having antibody titers to C. pneumoniae. The selected peptide mimotope sequences tended to be composed of charged residues surrounding a core of hydrophobic residues. The peptide with the best binding could inhibit >95% of binding to the MAb, suggesting that the selected peptide binds the paratope of the respective MAb. The peptide reacted with human sera previously determined by microimmunofluorescence to have anti-C. pneumoniae antibodies. The peptide was competitively competed with the MAb against Renografin-purified, sonicated C. pneumoniae in an enzyme-linked immunosorbent assay and with whole-cell C. pneumoniae in an indirect fluorescence assay format, demonstrating its potential utility in the development of diagnostics. The use of this novel peptide may allow investigators to establish standardized assays free from cross-reactive Chlamydia trachomatis and Chlamydophila psittaci epitopes and immunoreactivity.