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Journal of Bacteriology, September 2008, p. 5746-5752, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00391-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Lawsonia intracellularis Contains a Gene Encoding a Functional Rickettsia-Like ATP/ADP Translocase for Host Exploitation{triangledown}

Stephan Schmitz-Esser,1,{dagger} Ilka Haferkamp,2,{dagger} Silvia Knab,1 Thomas Penz,1 Michelle Ast,3 Christian Kohl,2 Michael Wagner,1 and Matthias Horn1*

Department für Mikrobielle Ökologie, Universität Wien, 1090 Vienna, Austria,1 Zelluläre Physiologie/Membrantransport, Technische Universität Kaiserslautern, 67653 Kaiserslautern, Germany,2 Pflanzenphysiologie, Technische Universität Kaiserslautern, 67653 Kaiserslautern, Germany3

Received 19 March 2008/ Accepted 26 June 2008

ATP/ADP translocases are a hallmark of obligate intracellular pathogens related to chlamydiae and rickettsiae. These proteins catalyze the highly specific exchange of bacterial ADP against host ATP and thus allow bacteria to exploit their hosts' energy pool, a process also referred to as energy parasitism. The genome sequence of the obligate intracellular pathogen Lawsonia intracellularis (Deltaproteobacteria), responsible for one of the most economically important diseases in the swine industry worldwide, revealed the presence of a putative ATP/ADP translocase most similar to known ATP/ADP translocases of chlamydiae and rickettsiae (around 47% amino acid sequence identity). The gene coding for the putative ATP/ADP translocase of L. intracellularis (L. intracellularis nucleotide transporter 1 [NTT1Li]) was cloned and expressed in the heterologous host Escherichia coli. The transport properties of NTT1Li were determined by measuring the uptake of radioactively labeled substrates by E. coli. NTT1Li transported ATP in a counterexchange mode with ADP in a highly specific manner; the substrate affinities determined were 236.3 (± 36.5) µM for ATP and 275.2 (± 28.1) µM for ADP, identifying this protein as a functional ATP/ADP translocase. NTT1Li is the first ATP/ADP translocase from a bacterium not related to Chlamydiae or Rickettsiales, showing that energy parasitism by ATP/ADP translocases is more widespread than previously recognized. The occurrence of an ATP/ADP translocase in L. intracellularis is explained by a relatively recent horizontal gene transfer event with rickettsiae as donors.

* Corresponding author. Mailing address: Universität Wien, Department für Mikrobielle Ökologie, Althanstr. 14, A-1090 Vienna, Austria. Phone: 43 1 4277 54393. Fax: 43 1 4277 54389. E-mail: horn{at}microbial-ecology.net

{triangledown} Published ahead of print on 7 July 2008.

{dagger} These authors contributed equally to this work.

Journal of Bacteriology, September 2008, p. 5746-5752, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00391-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ast, M., Gruber, A., Schmitz-Esser, S., Neuhaus, H. E., Kroth, P. G., Horn, M., Haferkamp, I. (2009). Diatom plastids depend on nucleotide import from the cytosol. Proc. Natl. Acad. Sci. USA 106: 3621-3626 [Abstract] [Full Text]  
  • Trentmann, O., Jung, B., Neuhaus, H. E., Haferkamp, I. (2008). Nonmitochondrial ATP/ADP Transporters Accept Phosphate as Third Substrate. J. Biol. Chem. 283: 36486-36493 [Abstract] [Full Text]  


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