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  • We found that a strains of Yersinia pestis (KIM5) which lacked the nhaA gene was fully attenuated in a plague model. This gene produces a protein of the sodium-proton antiporter family which expel sodium ions from the bacterial cytoplasm in exchange for hydrogen ions, or protons, from the surrounding environment. A Y. pestis strain that contained the nhaA mutation showed a significant decrease in its ability to survive in both sheep’s blood and serum. Decreased growth rates were also observed when the nhaA deficient strain was tested in the artificial serum media Opti-MEM® when compared to the wild type strain. A similar growth phenotype was observed when wild type and nhaA mutant strains were tested in LB media set to mimic pH and salt conditions of blood. These observations indicate that sodium-proton antiporter activity of Y. pestis is essential for the survival of the bacterium in certain environments, such as the blood of an infected host. 2-aminopyrimidine was used to inhibit NhaA activity, and when tested in Opti-MEM®, bacterial growth rates decreased. These findings lead us to propose that sodium-proton antiporter inhibition is a novel way of treating bacterial blood-borne diseases.
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  • description.provenance : Made available in DSpace on 2013-04-04T23:01:02Z (GMT). No. of bitstreams: 1 Poster Final.ppt: 745984 bytes, checksum: 61de8b93d323022a3e152245daa640d9 (MD5)
  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2013-04-04T23:01:02Z (GMT) No. of bitstreams: 1 Poster Final.ppt: 745984 bytes, checksum: 61de8b93d323022a3e152245daa640d9 (MD5)
  • description.provenance : Submitted by Wyatt Faulkner (faulknew@onid.orst.edu) on 2013-04-03T20:38:33Z No. of bitstreams: 1 Poster Final.ppt: 745984 bytes, checksum: 61de8b93d323022a3e152245daa640d9 (MD5)

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