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Summary  When the Lyme disease spirochete,  Borrelia burgdorferi , transfers from a feeding tick into a human or other vertebrate host, the bacterium produces vertebrate‐specific proteins and represses factors needed for arthropod colonization. Previous studies determined that the  B. burgdorferi  BpuR protein binds to its own mRNA and autoregulates its translation, and also serves as co‐repressor of  erp  transcription. Here, we demonstrate that  B. burgdorferi  controls transcription of  bpuR , expressing high levels of  bpuR  during tick colonization but significantly less during mammalian infection. The master regulator of chromosomal replication, DnaA, was found to bind specifically to a DNA sequence that overlaps the  bpuR  promoter. Cultured  B. burgdorferi  that were genetically manipulated to produce elevated levels of BpuR exhibited altered levels of several proteins, although BpuR did not impact mRNA levels. Among these was the SodA superoxide dismutase, which is essential for mammalian infection. BpuR bound to  sodA  mRNA in live  B. burgdorferi , and a specific BpuR‐binding site was mapped 5′ of the  sodA  open reading frame. Recognition of posttranscriptional regulation of protein levels by BpuR adds another layer to our understanding of the  B. burgdorferi  regulome, and provides further evidence that bacterial protein levels do not always correlate directly with mRNA levels.

molecular microbiology

The Lyme disease spirochete's BpuR DNA/RNA‐binding protein is differentially expressed during the mammal–tick infectious cycle, which affects translation of the SodA superoxide dismutase