“
“Streptococcal histidine triad protein was identified recently as a cell surface-associated protein family. Five members of this family (PhtA, PhtB, PhtD, PhtE and HtpA), derived from Streptococcus pneumoniae and Streptococcus pyogenes, have been shown as antigens that confer protection to the host on infection. In this report, a gene sequence highly homologous to htpA and phtD (designated htpS, the histidine triad protein of Streptococcus suis) was identified from S. suis 2 Chinese strain 05ZYH33. Our data revealed that htpS is extremely conserved in S. suis 2 and widely distributed in 83% (29/35)

of 35 S. suis serotypes. It was also demonstrated by Western blot and flow cytometry that HtpS is a cell surface-associated protein that was expressed during S. suis 2 infection. An antibody against HtpS could increase the deposition of human GSK2118436 ic50 complement 3 on S. suis 2 and also enhance the clearance of S. suis 2 in whole blood. In addition, Regorafenib mice could be immunized against S. suis 2 infection and were well protected after immunization with recombinant HtpS.

Streptococcus suis is an important Gram-positive pathogenic bacterium that can infect piglets and cause many serious diseases such as arthritis, meningitis and septicemia (Lun et al., 2007). It is also an important zoonotic agent for individuals who are in contact with infected swine or healthy carriers (Wertheim et al., 2009). To date, 35 serotypes (types 1/2 and 1–34) of S. suis have been described. Streptococcus suis serotype 2 (S. suis 2) is the most frequently isolated and associated with disease (Higgins & Gottschalk, 1995; Messier et al., 2008). Two outbreaks of severe human S. suis 2 infections in China were characterized by streptococcal toxic shock syndrome in 1998 and 2005, which caused mortality of up to 62.7% and 81.3%, respectively (Tang et al., 2006). This suggested that the prevention and Cell press control of the S. suis 2 infection has become an urgent task in such a grim situation. However, effective control of S. suis 2 infection

was lacking due to the absence of safe and effective vaccines (Haesebrouck et al., 2004). It is well recognized that sequence-conserved, surface-exposed bacterial proteins could be considered as vaccine candidates for subunit vaccine development (Etz et al., 2002; Hamel et al., 2004; Timoney et al., 2007). Based on the sequencing of two virulent S. suis 2 genomes (Chen et al., 2007), a collection of structural and enzymatic proteins that are associated with the bacterial cell wall have been identified from the highly pathogenic isolates (Feng et al., 2007, 2009; Li et al., 2007; Esgleas et al., 2008; Ge et al., 2009; Wang et al., 2009; Zhang et al., 2009). Recently, a study of the divalent-cation-regulated cell surface-associated proteins of S. suis 2 identified several immunogenic proteins in the adcR mutation of S.