Intracellular Concentrations of Borrelia burgdorferi Cyclic Di-AMP Are Not Changed by Altered Expression of the CdaA Synthase

PLoS One. 2015 Apr 23;10(4):e0125440. doi: 10.1371/journal.pone.0125440. eCollection 2015.

Abstract

The second messenger nucleotide cyclic diadenylate monophosphate (c-di-AMP) has been identified in several species of Gram positive bacteria and Chlamydia trachomatis. This molecule has been associated with bacterial cell division, cell wall biosynthesis and phosphate metabolism, and with induction of type I interferon responses by host cells. We demonstrate that B. burgdorferi produces a c-di-AMP synthase, which we designated CdaA. Both CdaA and c-di-AMP levels are very low in cultured B. burgdorferi, and no conditions were identified under which cdaA mRNA was differentially expressed. A mutant B. burgdorferi was produced that expresses high levels of CdaA, yet steady state borrelial c-di-AMP levels did not change, apparently due to degradation by the native DhhP phosphodiesterase. The function(s) of c-di-AMP in the Lyme disease spirochete remains enigmatic.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Borrelia burgdorferi / enzymology*
  • Borrelia burgdorferi / metabolism
  • Cyclic AMP / metabolism*
  • Gene Expression Regulation, Bacterial
  • Phosphoric Diester Hydrolases / metabolism
  • Proteomics / methods

Substances

  • Bacterial Proteins
  • Cyclic AMP
  • Phosphoric Diester Hydrolases

Grants and funding

Funded by an exploratory grant from the University of Kentucky College of Medicine to B. Stevenson, and National Science Foundation grant MCB1253684 to CMW. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.