TY - JOUR
T1 - HtrA is important for stress resistance and virulence in haemophilus parasuis
AU - Zhang, Luhua
AU - Li, Ying
AU - Wen, Yiping
AU - Lau, Gee W.
AU - Huang, Xiaobo
AU - Wu, Rui
AU - Yan, Qigui
AU - Huang, Yong
AU - Zhao, Qin
AU - Ma, Xiaoping
AU - Wen, Xintian
AU - Caoa, Sanjie
N1 - Publisher Copyright:
© 2016 Zhang et al.
PY - 2016
Y1 - 2016
N2 - Haemophilus parasuis is an opportunistic pathogen that causes Glässer's disease in swine, with polyserositis, meningitis, and arthritis. The high-temperature requirement A (HtrA)-like protease, which is involved in protein quality control, has been reported to be a virulence factor in many pathogens. In this study, we showed that HtrA of H. parasuis (HpHtrA) exhibited both chaperone and protease activities. Finally, nickel import ATP-binding protein (NikE), periplasmic dipeptide transport protein (DppA), and outer membrane protein A (OmpA) were identified as proteolytic substrates for HpHtrA. The protease activity reached its maximum at 40°C in a time-dependent manner. Disruption of the htrA gene from strain SC1401 affected tolerance to temperature stress and resistance to complement-mediated killing. Furthermore, increased autoagglutination and biofilm formation were detected in the htrA mutant. In addition, the htrA mutant was significantly attenuated in virulence in the murine model of infection. Together, these data demonstrate that HpHtrA plays an important role in the virulence of H. parasuis.
AB - Haemophilus parasuis is an opportunistic pathogen that causes Glässer's disease in swine, with polyserositis, meningitis, and arthritis. The high-temperature requirement A (HtrA)-like protease, which is involved in protein quality control, has been reported to be a virulence factor in many pathogens. In this study, we showed that HtrA of H. parasuis (HpHtrA) exhibited both chaperone and protease activities. Finally, nickel import ATP-binding protein (NikE), periplasmic dipeptide transport protein (DppA), and outer membrane protein A (OmpA) were identified as proteolytic substrates for HpHtrA. The protease activity reached its maximum at 40°C in a time-dependent manner. Disruption of the htrA gene from strain SC1401 affected tolerance to temperature stress and resistance to complement-mediated killing. Furthermore, increased autoagglutination and biofilm formation were detected in the htrA mutant. In addition, the htrA mutant was significantly attenuated in virulence in the murine model of infection. Together, these data demonstrate that HpHtrA plays an important role in the virulence of H. parasuis.
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U2 - 10.1128/IAI.00147-16
DO - 10.1128/IAI.00147-16
M3 - Article
C2 - 27217419
AN - SCOPUS:84979790721
SN - 0019-9567
VL - 84
SP - 2209
EP - 2219
JO - Infection and immunity
JF - Infection and immunity
IS - 8
ER -