Immunoreactive proteins of Ehrlichia canis and Ehrlichia chaffeensis that have been characterized include a family of 28-kDa major outer membrane proteins (p28) and two large antigenically divergent surface glycoprotein orthologs. We previously demonstrated that recombinant E. canis p28 and the 140-and 200-kDa glycoproteins gp140 and gp200, respectively, react strongly with serum antibodies from suspect canine ehrlichiosis cases that were positive for E. canis by immunofluorescent antibody test and in various phases of acute or chronic infection (J. Clin. Microbiol. 39:315-322, 2001). The kinetics of the antibody response to these potentially important vaccine and immunodiagnostic candidates is not known. Acute-phase serum antibody responses to whole-cell E. canis lysates and recombinant p28, gp140, and gp200 were monitored for 6 weeks in dogs experimentally infected with E. canis. Irrespective of the inoculation route, a T-helper 1-type response was elicited to E. canis antigens consisting of immunoglobulin G2 antibodies exclusively in both acute and convalescent phases in most dogs. Analysis of immuoreactive antigens for peak intensity and relative quantity identified major immunoreactive E. canis antigens recognized early in the infection as the 19-, 37-, 75-, and 140-kDa proteins. Later in infection, additional major immunoreactive E. canis proteins were identified, including the 28-, 47-, and 95-kDa proteins and the recently identified 200-kDa glycoprotein. All dogs had developed antibody against the recombinant gp140, gp200, and p28 in the convalescent phase. Immunoreactivity and antibody response kinetics suggest that major immunoreactive proteins identified are immunodominant, but early recognition suggests increased dominance by some antigens.

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These data showed a clear association of spiroplasma with scrapie suggesting that these bacteria have a role in the pathogenesis of TSE and that the eye should be a research focus for future studies of TSE.

In vitro, cecropin B has an effective antibacterial activity against M. haemolytica S1 and can prevent colonization of the nasal mucosa after transfection of a vector expressing cecropin B in vivo.

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