Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis

PLoS One. 2017 May 11;12(5):e0176396. doi: 10.1371/journal.pone.0176396. eCollection 2017.

Abstract

The whooping cough agent Bordetella pertussis controls the expression of its large virulence regulon in a coordinated manner through the two-component signal transduction system BvgAS. In addition to the genes coding for bona fide virulence factors, the Bvg regulon comprises genes of unknown function. In this work, we characterized a new Bvg-activated gene called BP2936. Homologs of BP2936 are found in other pathogenic Bordetellae and in several other species, including plant pathogens and environmental bacteria. We showed that the gene product of BP2936 is a membrane-associated methyl-transferase of free fatty acids. We thus propose to name it FmtB, for fatty acid methyl-transferase of Bordetella. The role of this protein was tested in cellular and animal models of infection, but the loss of BP2936 did not appear to affect host-pathogen interactions in those assays. The high level of conservation of BP2936 among B. pertussis isolates nevertheless argues that it probably plays a role in the life cycle of this pathogen.

MeSH terms

  • Bacterial Proteins / genetics
  • Bordetella pertussis / enzymology
  • Bordetella pertussis / genetics*
  • Bordetella pertussis / pathogenicity
  • Fatty Acids, Nonesterified / genetics
  • Gene Expression Regulation, Bacterial
  • Host-Pathogen Interactions / genetics
  • Humans
  • Methyltransferases / genetics*
  • Regulon / genetics
  • Signal Transduction
  • Virulence Factors, Bordetella / genetics*
  • Whooping Cough / genetics*
  • Whooping Cough / microbiology

Substances

  • Bacterial Proteins
  • BvgB protein, Bordetella pertussis
  • Fatty Acids, Nonesterified
  • Virulence Factors, Bordetella
  • Methyltransferases
  • fatty acid methyltransferase

Grants and funding

This work was supported by the recurrent funding of our laboratory (INSERM, Lille University). We also acknowledge the participation of the UMR 8199 LIGAN-PM Genomics platform (Lille, France), which belongs to the 'Federation de Recherche' 3508 Labex EGID (European Genomics Institute for Diabetes; ANR-10-LABX-46) and was supported by the ANR Equipex 2010 session (ANR-10-EQPX-07-01; 'LIGAN-PM'). The LIGAN-PM Genomics platform (Lille, France) is also supported by the FEDER and the Region Nord-Pas-de-Calais-Picardie. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.