000184454 001__ 184454
000184454 005__ 20190316235557.0
000184454 0247_ $$2doi$$a10.1371/journal.pone.0043467
000184454 022__ $$a1932-6203
000184454 02470 $$2ISI$$a000308063700109
000184454 037__ $$aARTICLE
000184454 245__ $$aA Point Mutation in cycA Partially Contributes to the D-cycloserine Resistance Trait of Mycobacterium bovis BCG Vaccine Strains
000184454 269__ $$a2012
000184454 260__ $$bPublic Library of Science$$c2012$$aSan Francisco
000184454 300__ $$a7
000184454 336__ $$aJournal Articles
000184454 520__ $$aIn mycobacteria, CycA a D-serine, L-and D-alanine, and glycine transporter also functions in the uptake of D-cycloserine, an important second-line anti-tubercular drug. A single nucleotide polymorphism identified in the cycA gene of BCG was hypothesized to contribute to the increased resistance of Mycobacterium bovis bacillus Calmette-Guerin (BCG) to D-cycloserine compared to wild-type Mycobacterium tuberculosis or Mycobacterium bovis. Working along these lines, a merodiploid strain of BCG expressing Mycobacterium tuberculosis CycA was generated and found to exhibit increased susceptibility to D-cycloserine albeit not to the same extent as wild-type Mycobacterium tuberculosis or Mycobacterium bovis. In addition, recombinant Mycobacterium smegmatis strains expressing either Mycobacterium tuberculosis or Mycobacterium bovis CycA but not BCG CycA were rendered more susceptible to D-cycloserine. These findings support the notion that CycA-mediated uptake in BCG is impaired as a result of a single nucleotide polymorphism; however, the partial contribution of this impairment to D-cycloserine resistance suggests the involvement of additional genetic lesions in this phenotype.
000184454 700__ $$uEcole Polytech Fed Lausanne, Global Hlth Inst, Lausanne, Switzerland$$aChen, Jeffrey M.
000184454 700__ $$0244370$$g181909$$uEcole Polytech Fed Lausanne, Global Hlth Inst, Lausanne, Switzerland$$aUplekar, Swapna
000184454 700__ $$uUniv Coll Dublin, Sch Vet Med, Dublin 2, Ireland$$aGordon, Stephen V.
000184454 700__ $$uEcole Polytech Fed Lausanne, Global Hlth Inst, Lausanne, Switzerland$$aCole, Stewart T.$$g177247$$0243892
000184454 773__ $$j7$$tPlos One$$k8$$qe43467
000184454 8564_ $$uhttps://infoscience.epfl.ch/record/184454/files/journal.pone.0043467.pdf$$zPublisher's version$$s1065935$$yPublisher's version
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000184454 937__ $$aEPFL-ARTICLE-184454
000184454 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000184454 980__ $$aARTICLE