Open AccessIntracellular Concentrations of Borrelia burgdorferi Cyclic Di-AMP Are Not Changed by Altered Expression of the CdaA Synthase
Author(s) -
Christina R. Savage,
William K. Arnold,
Alexandra Gjevre-Nail,
Benjamin J. Koestler,
Eric L. Bruger,
Jeffrey R. Barker,
Christopher M. Waters,
Brian Stevenson
Publication year - 2015
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0125440
Subject(s) - borrelia burgdorferi , intracellular , biology , chlamydia trachomatis , atp synthase , nucleotide , bacteria , microbiology and biotechnology , biochemistry , enzyme , genetics , virology , gene , antibody
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.