The QseB/QseC two-component system contributes to virulence of Actinobacillus pleuropneumoniae by downregulating apf gene cluster transcription

Actinobacillus pleuropneumoniae (APP) is the major pathogen of porcine contagious pleuropneumoniae (PCP). The QseB/QseC two-component system (TCS) consists of the regulator QseB and the kinase QseC, which relates to quorum sensing (QS) and virulence in some bacteria. Here, we investigated the role o...

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Veröffentlicht in:Animal diseases 2022-01, Vol.2 (1), p.1-12, Article 2
Hauptverfasser: Duan, Benzhen, Peng, Wei, Yan, Kang, Liu, Feng, Tang, Jia, Yang, Fengming, Chen, Huanchun, Yuan, Fangyan, Bei, Weicheng
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Sprache:eng
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Zusammenfassung:Actinobacillus pleuropneumoniae (APP) is the major pathogen of porcine contagious pleuropneumoniae (PCP). The QseB/QseC two-component system (TCS) consists of the regulator QseB and the kinase QseC, which relates to quorum sensing (QS) and virulence in some bacteria. Here, we investigated the role of QseB/QseC in apf gene cluster ( apfABCD ) expression of APP. Our results have showed that QseB/QseC TCS can potentially regulate the expression of apf gene cluster. The Δ qseBC , Δ apfA , Δ apfB , Δ apfC and Δ apfD strains are more sensitive to acidic and osmotic stressful conditions, and exhibite lower biofilm formation ability than wild-type (WT) strain, whereas the complemented strains show similar phenotype to the WT strain. In additon, the mutants have defective anti-phagocytosis, adhesion and invasion when they come into contact with the host cells. In experimental animal models of infection, mice infected with Δ qseBC , Δ apfA , Δ apfB , Δ apfC and Δ apfD strains showed lower mortality and bacterial loads in the lung and the blood than those infected with WT strain. In conclusion, our results suggest that QseB/QseC TCS contributes to stress resistance, biofilm formation, phagocytosis, adhesion, invasion and virulence by downregulating expression of apf gene cluster in A. pleuropneumoniae .
ISSN:2731-0442
2731-0442
DOI:10.1186/s44149-022-00036-w