Intracellular concentrations of Borrelia burgdorferi cyclic di-AMP are not changed by altered expression of the CdaA synthase

Christina R. Savage, William K. Arnold, Alexandra Gjevre-Nail, Benjamin J. Koestler, Eric L. Bruger, Jeffrey R. Barker, Christopher M. Waters, Brian Stevenson

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

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 cdi-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.

Original languageEnglish
Article numbere0125440
JournalPLoS ONE
Volume10
Issue number4
DOIs
StatePublished - Apr 23 2015

Bibliographical note

Publisher Copyright:
© 2015 Savage et al.

ASJC Scopus subject areas

  • General

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