The phosphocarrier protein HPr of Neisseria meningitidis interacts with the transcription regulator CrgA and its deletion affects capsule production, cell adhesion, and virulence

• DOI: 10.1111/mmi.13349
• Publication Date: 2016-02-09T09:05:54Z
• Authors: Meriem Derkaoui; Ana Antunes; Sandrine Poncet; Jamila Nait Abdallah; Philippe Joyet; Alain Mazé; Céline Henry; Muhamed‐Kheir Taha; Josef Deutscher; Ala‐Eddine Deghmane
• Keywords: PEP group translocation; Transcription

The bacterial phosphotransferase system (PTS) transports and phosphorylates sugars, but also carries out numerous regulatory functions. β-proteobacterium Neisseria meningitidis possesses an incomplete PTS unable to transport carbon sources because it lacks a membrane component. Nevertheless, the residual phosphorylation cascade is functional meningococcal was therefore expected carry roles. Interestingly, ΔptsH mutant (lacks protein HPr) exhibited reduced virulence in mice after intraperitoneal challenge rapidly cleared from bloodstream of BALB/c mice. rapid clearance correlates with lower capsular polysaccharide production by mutant, which probably responsible for its increased adhesion Hec-1-B epithelial cells. In addition, compared wild-type strain more apoptotic cells were detected when infected strain. Coimmunoprecipitation revealed interaction HPr P-Ser-HPr LysR type transcription regulator CrgA, among others controls own expression. Moreover, ptsH deletion caused expression ΦcrgA-lacZ fusion. Finally, presence or phospho-HPr's during electrophoretic mobility shift assays enhanced affinity CrgA target sites preceding crgA pilE, did not promote binding sia pilC1 promoter regions.