Rv2190c, an NlpC/P60 family protein, is required for full virulence of Mycobacterium tuberculosis

PLoS One. 2012;7(8):e43429. doi: 10.1371/journal.pone.0043429. Epub 2012 Aug 31.

Abstract

Mycobacterium tuberculosis, the etiologic agent of tuberculosis (TB) possesses at least five genes predicted to encode proteins with NlpC/P60 hydrolase domains, including the relatively uncharacterized Rv2190c. As NlpC/P60 domain-containing proteins are associated with diverse roles in bacterial physiology, our objective was to characterize Rv2190c in M. tuberculosis growth and virulence. Our data indicate that lack of Rv2190c is associated with impaired growth, both in vitro and during an in vivo mouse model of TB. These growth defects are associated with altered colony morphology and phthiocerol dimycocerosate levels, indicating that Rv2190c is involved in cell wall maintenance and composition. In addition, we have demonstrated that Rv2190c is expressed during active growth phase and that its protein product is immunogenic during infection. Our findings have significant implications, both for better understanding the role of Rv2190c in M. tuberculosis biology and also for translational developments.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Female
  • Gene Expression Regulation, Bacterial*
  • Genetic Complementation Test
  • Lipids / chemistry
  • Mice
  • Mice, Inbred BALB C
  • Microscopy, Electron, Transmission / methods
  • Muramidase / chemistry
  • Mutation
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / metabolism*
  • Phenotype
  • Protein Biosynthesis
  • Tuberculosis / metabolism
  • Tuberculosis / parasitology*
  • Virulence
  • Virulence Factors / genetics*
  • Virulence Factors / metabolism

Substances

  • Bacterial Proteins
  • Lipids
  • Rv2190c protein, Mycobacterium tuberculosis
  • Virulence Factors
  • phthiocerol dimycocerosate
  • Muramidase