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Neorickettsia risticii  is the Gram-negative, obligate, and intracellular bacterial pathogen responsible for Potomac horse fever (PHF): an important acute systemic disease of horses.  N. risticii  surface proteins, critical for immune recognition, have not been thoroughly characterized. In this paper, we identified the 51-kDa antigen (P51) as a major surface-exposed outer membrane protein of older and contemporary strains of  N. risticii  through mass spectrometry of streptavidin-purified biotinylated surface-labeled proteins. Western blot analysis of sera from naturally-infected horses demonstrated universal and strong recognition of recombinant P51 over other  Neorickettsia  recombinant proteins. Comparisons of amino acid sequences for predicted secondary structures of P51, as well as  Neorickettsia  surface proteins 2 (Nsp2) and 3 (Nsp3) among  N. risticii  strains from horses with PHF during a 26-year period throughout the United States revealed that the majority of variations among strains were concentrated in regions predicted to be external loops of their β-barrel structures. Large insertions or deletions occurred within a tandem-repeat region in Ssa3. These data demonstrate patterns of geographical association for P51 and temporal associations for Nsp2, Nsp3, and Ssa3, indicating evolutionary trends for these  Neorickettsia  surface antigen genes. This study showed  N. risticii  surface protein population dynamics, providing groundwork for designing immunodiagnostic targets for PHF.

Neorickettsia risticii surface-exposed proteins: proteomics identification, recognition by naturally-infected horses, and strain variations