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Characterization of the Na+/H+ Antiporter from Yersinia pestis

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  • Assaf Ganoth
  • Raphael Alhadeff
  • Dovrat Kohen
  • Isaiah T Arkin

Abstract

Yersinia pestis, the bacterium that historically accounts for the Black Death epidemics, has nowadays gained new attention as a possible biological warfare agent. In this study, its Na/H antiporter is investigated for the first time, by a combination of experimental and computational methodologies. We determined the protein's substrate specificity and pH dependence by fluorescence measurements in everted membrane vesicles. Subsequently, we constructed a model of the protein's structure and validated the model using molecular dynamics simulations. Taken together, better understanding of the Yersinia pestis Na/H antiporter's structure-function relationship may assist in studies on ion transport, mechanism of action and designing specific blockers of Na/H antiporter to help in fighting Yersinia pestis -associated infections. We hope that our model will prove useful both from mechanistic and pharmaceutical perspectives.

Suggested Citation

  • Assaf Ganoth & Raphael Alhadeff & Dovrat Kohen & Isaiah T Arkin, 2011. "Characterization of the Na+/H+ Antiporter from Yersinia pestis," PLOS ONE, Public Library of Science, vol. 6(11), pages 1-9, November.
    • Handle: RePEc:plo:pone00:0026115
    DOI: 10.1371/journal.pone.0026115
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    References listed on IDEAS

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    1. Carola Hunte & Emanuela Screpanti & Miro Venturi & Abraham Rimon & Etana Padan & Hartmut Michel, 2005. "Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH," Nature, Nature, vol. 435(7046), pages 1197-1202, June.
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