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      Interaction of the Lyme disease spirochete with its tick vector

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          Summary

          Borrelia burgdorferi , the causative agent of Lyme disease (along with closely related genospecies), is in the deeply branching spirochete phylum. The bacterium is maintained in nature in an enzootic cycle that involves transmission from a tick vector to a vertebrate host and acquisition from a vertebrate host to a tick vector. During its arthropod sojourn, B. burgdorferi faces a variety of stresses, including nutrient deprivation. Here, we review some of the spirochetal factors that promote persistence, maintenance and dissemination of B. burgdorferi in the tick, and then focus on the utilization of available carbohydrates as well as the exquisite regulatory systems invoked to adapt to the austere environment between blood meals and to signal species transitions as the bacteria traverse their enzootic cycle. The spirochetes shift their source of carbon and energy from glucose in the vertebrate to glycerol in the tick. Regulation of survival under limiting nutrients requires the classic stringent response in which Rel Bbu controls the levels of the alarmones guanosine tetraphosphate and guanosine pentaphosphate (collectively termed (p)ppGpp), while regulation at the tick–vertebrate interface as well as regulation of protective responses to the blood meal require the two-component system Hk1/Rrp1 to activate production of the second messenger cyclic-dimeric-GMP (c-di-GMP).

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          Author and article information

          Journal
          100883691
          21720
          Cell Microbiol
          Cell. Microbiol.
          Cellular microbiology
          1462-5814
          1462-5822
          12 October 2016
          24 May 2016
          July 2016
          17 October 2016
          : 18
          : 7
          : 919-927
          Affiliations
          [1 ]Departments of Medicine, Pediatrics, and Molecular Biology and Biophysics, UConn Health, Farmington, CT, USA
          [2 ]Division of Biological Sciences, University of Montana, Missoula, MT, USA
          [3 ]Department of Veterinary Medicine, University of Maryland–College Park and Virginia–Maryland Regional College of Veterinary Medicine, College Park, MD, USA
          [4 ]Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, USA
          Author notes
          [* ]For correspondence: scott.samuels@ 123456umontana.edu ; Tel. (406) 243-6145; Fax (406) 243-4184
          Article
          PMC5067140 PMC5067140 5067140 nihpa822254
          10.1111/cmi.12609
          5067140
          27147446
          b81423ec-f2ad-4040-a264-0c75089f5a31
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