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Immunomolecular characterization of  Ehrlichia chaffeensis  ( E. ch .) and  E. canis  ( E. ca .) has defined protein orthologs, including tandem repeat proteins (TRPs) that have immunodominant linear antibody epitopes. In this study, we combined bioinformatic analysis and cell-free protein expression to identify undiscovered immunoreactive  E. ch . and  E. ca . hypothetical proteins. Antigenicity of the  E. ch . and  E. ca . ORFeomes ( n  = 1105 and  n  = 925, respectively) was analyzed by the sequence-based prediction model ANTIGENpro, and we identified ~250 ORFs in each respective ORFeome as highly antigenic. The hypothetical proteins ( E. ch .  n  = 93 and  E. ca .  n  = 98) present in the top 250 antigenic ORFs were further investigated in this study. By ELISA, 46  E. ch . and 30  E. ca . IVTT-expressed hypothetical proteins reacted with antibodies in sera from naturally  E. ch .-infected patients or  E. ca .-infected dogs. Moreover, 15  E. ch . and 16  E. ca . proteins consistently reacted with a panel of sera from patients or dogs, including many that revealed the immunoreactivity of “gold standard” TRPs. Antibody epitopes in most (>70%) of these proteins exhibited partial or complete conformation-dependence. The majority (23/31; 74%) of the major immunoreactive proteins identified were small (≤250 aa), and 20/31 (65%) were predicted to be secreted effectors. Unlike the strong linear antibody epitopes previously identified in TRP and OMP orthologs, there were contrasting differences in the  E. ch . and  E. ca . antigenic repertoires, epitopes and ortholog immunoreactivity. This study reveals numerous previously undefined immunodominant and subdominant antigens, and illustrates the breadth, complexity, and diversity of immunoreactive proteins/epitopes in  Ehrlichia .

npj vaccines

Ehrlichia chaffeensis and E. canis hypothetical protein immunoanalysis reveals small secreted immunodominant proteins and conformation-dependent antibody epitopes