Immunization with truncated recombinant protein SpaC of Erysipelothrix rhusiopathiae strain 715 serovar 18 confers protective immunity against challenge with various serovars.

摘要: Previously, we showed that surface protective antigen (Spa) proteins of Erysipelothrix rhusiopathiae can be classified into three molecular species—SpaA, SpaB, and SpaC—and SpaC is the most broadly cross-protective among Spa proteins. In this study, examined ability α-helical domain, which comprises N-terminal half SpaC, to elicit immunity in mice pigs. Mice actively immunized with full-length protein (rSpaC664) or domain (rSpaC427), but not C-terminal (rSpaC253), were protected against challenge E. serovars 1a, 2, 6, 19, 18 expressing heterologous (SpaA SpaB) homologous (SpaC) Spas. The seemed provide better protection than rSpaC664, although differences did reach statistical significance. Similarly, passively rabbit anti-rSpaC664 anti-rSpaC427 sera, anti-rSpaC253 serum, from various serovars. Pigs SpaC427 also developed specific antibodies highly virulent strain Fujisawa (serovar 1a). Taken together, these results demonstrate for first time striking efficacy domain-mediated immunization both pigs, thereby highlighting its utility as promising candidate development a safe effective vaccine erysipelas.