1. Molecular and functional characterization of HtrA protein in Actinobacillus pleuropneumoniae
- Author
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Qin Zhao, Rui Wu, Hong-Ze Jiang, Xin-Ran Mou, Yu-Qin Cao, Xiaobo Huang, Yiping Wen, Chang Miao, Sen-Yan Du, Kui Xu, Qigui Yan, Yung-Fu Chang, and Sanjie Cao
- Subjects
Swine ,animal diseases ,medicine.medical_treatment ,Spleen ,Microbiology ,Antigen ,Heat shock protein ,medicine ,Animals ,HSP90 Heat-Shock Proteins ,Actinobacillus pleuropneumoniae ,Swine Diseases ,Mice, Inbred BALB C ,Protease ,General Veterinary ,biology ,Serine Endopeptidases ,General Medicine ,respiratory system ,Th1 Cells ,bacterial infections and mycoses ,biology.organism_classification ,Hsp90 ,respiratory tract diseases ,Disease Models, Animal ,medicine.anatomical_structure ,Chaperone (protein) ,Immunoglobulin G ,Proteolysis ,biology.protein ,Female ,Bacterial outer membrane ,Bacterial Outer Membrane Proteins - Abstract
Actinobacillus pleuropneumoniae (A.pleuropneumoniae) causes serious economic loss for the swine industry. A high-temperature requirements A (HtrA)-like protease and its homologs have been reported to be involved in protein quality control and expression of important immunoprotective antigens in many pathogens. In this study, we showed that HtrA of A.pleuropneumoniae exhibited both chaperone and proteolytic activities. Moreover, Outer membrane protein P5 (OmpP5) in A.pleuropneumoniae and Heat shock protein 90 (Hsp90) in porcine lung tissues were first discovered and identified as specific proteolytic substrates for rHtrA. The maximum cleavage activity occurs at 50 ℃ in a time-dependent manner. In addition, rHtrA mainly induced IgG 2a subtype of IgG and Th1 (IFN-γ, IL-2) response in a mice model, and promoted a significant proliferation of spleen lymphocytes compare with negative control (P < 0.05). The survival rates of 37.5 % were observed against A.pleuropneumoniae strain. Together, these data demonstrate that rHtrA plays a multi-functional role in A.pleuropneumoniae.
- Published
- 2020