Identification and characterization of epitopes on the 120-kilodalton surface protein antigen of Rickettsia prowazekii with synthetic peptides.

Infection and Immunity
W M ChingG A Dasch

Abstract

The 120-kDa surface protein antigens (SPAs) of typhus rickettsiae are highly immunogenic and have been shown to be responsible for the species-specific serological reactions of the typhus group rickettsiae. To study the immunochemistry of these proteins, overlapping decapeptides encompassing the whole protein were synthesized on derivatized polyethylene pins. A modified enzyme-linked immunosorbent assay was used to identify epitopes recognized by rabbit hyperimmune antisera to Rickettsia prowazekii SPA. Eight distinct epitopes were mapped by this method in three regions. Four of the epitopes, which were located in the carboxyterminus of mature processed SPA, were strongly competitively inhibited by native folded SPA but not by intact rickettsiae, suggesting that they were on the SPA surface but not exposed on the rickettsial surface. Three of these epitopes were present on both R. prowazekii and Rickettsia typhi SPAs. The immunoreactivities of five epitopes were further characterized by synthesizing modified peptides. Glycine substitution experiments determined the critical residues in the epitopes. The dependence of binding of the peptide epitopes to the polyclonal antisera was mapped to single residues. The limited number and...Continue Reading

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Citations

Apr 17, 2008·Nature Reviews. Microbiology·David H Walker, Nahed Ismail
Dec 30, 2016·Journal of Bacteriology·Nicholas F NorieaTed Hackstadt
Feb 17, 2006·Annals of the New York Academy of Sciences·Maxime NgwamidibaPierre-Edouard Fournier
Jun 24, 2005·Molecular Biology and Evolution·Guillaume BlancDidier Raoult
Oct 23, 2020·PLoS Neglected Tropical Diseases·Anke Osterloh
Mar 1, 2006·BMC Microbiology·Maxime NgwamidibaPierre-Edouard Fournier

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