suis 2 of 110 kDa (Fig. 2b), confirming that HtpS is a cell surface-associated protein of S. suis 2. To determine whether rHtpS-elicited antibodies could affect C3 deposition on the surface of S. suis 2, 05ZYH33 binding of C3 was detected by FCM after incubation with different concentrations of rabbit anti-HtpS sera. C3 deposition on S. suis 2 was low (41.9±2.01%) in the absence of rabbit anti-HtpS sera. When S. suis 2 was incubated with increasing concentrations of rabbit anti-HtpS sera, the C3 deposition on the bacterial surface was increased significantly in a rabbit anti-HtpS sera concentration-dependent manner, with up to 62.9±4.20% bacteria positive

with 50% rabbit anti-HtpS Dasatinib in vivo sera (Fig. 4). Normal human sera and preimmune rabbit sera

were used as controls and induced only weak changes in C3 deposition compared with rabbit anti-HtpS sera (data not shown). The bactericidal experiment was adopted to evaluate the bactericidal activity of the rabbit anti-HtpS antibody. As shown in Fig. 5, 72.9±3.88% of S. suis 2 bacteria could survive after incubation with whole blood not containing rabbit anti-HtpS antibody. In the presence of 5% rabbit anti-HtpS antibody, the survival of the bacteria in whole blood was significantly reduced to 51±7.74%. To determine Talazoparib clinical trial whether rHtpS can protect mice against S. suis 2 infection, mice were immunized with rHtpS and challenged with a lethal dose of S. suis 2 05ZYH33. ELISA test results revealed that titers of rHtpS-specific antibody of the group immunized with rHtpS ranged from 204 800 to 819 200 before challenge with S. suis 2. After the challenge, all 10 mice of the negative control group died

within 24 h postinoculation, while only two out of 10 mice immunized with rHtpS died in the same period. The remaining eight mice only exhibited rough hair in the first 24 h postinoculation, and then recovered and survived (Fig. 6). The mortality rate was significantly reduced in mice immunized with rHtpS (P<0.001), indicating that rHtpS confers protection in mice. So far, histidine triad family proteins have been documented in group A, B, C, G streptococcal species, S. pneumoniae, as well as S. suis 2 (Adamou et al., 2001; Kunitomo et al., 2008; Aranda et al., 2009). Mirabegron Although the function of this family is not clear, histidine triad protein family members, Pht proteins of S. pneumoniae and HtpA of S. pyogenes, have proved to be good candidates for subunit vaccines due to their strong ability to protect mice against bacterial infection (Adamou et al., 2001; Zhang et al., 2001; Kunitomo et al., 2008). Crystal structure analysis of PhtA revealed that the histidine triad domain of histidine triad protein family members was a zinc-binding fold (Riboldi-Tunnicliffe et al., 2004, 2005). Recently, Ogunniyi et al.