4.8 Article

Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate

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NATURE CHEMICAL BIOLOGY
卷 9, 期 11, 页码 674-+

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NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1355

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资金

  1. Agence Nationale de la Recherche
  2. UK Medical Research Council [MC_UP_A253_1111]
  3. European Union [241745]
  4. Region Midi-Pyrenees (Contrat de Projets Etat-Region Midi-Pyrenees (CPER))
  5. Grand Toulouse community
  6. Agence pour la Recherche sur le Cancer (ARC) [8505]
  7. Centre National de la Recherche Scientifique
  8. European Union-European Regional Development Fund program
  9. Fondation pour la Recherche Medicale
  10. MRC [MC_UP_A253_1111, MR/J006874/1] Funding Source: UKRI
  11. Medical Research Council [MC_UP_A253_1111] Funding Source: researchfish

向作者/读者索取更多资源

Here we identify the amino acid transporter AnsP1 as the unique aspartate importer in the human pathogen Mycobacterium tuberculosis. Metabolomic analysis of a mutant with an inactive AnsP1 revealed that the transporter is essential for M. tuberculosis to assimilate nitrogen from aspartate. Virulence of the AnsP1 mutant is impaired in vivo, revealing that aspartate is a primary nitrogen source required for host colonization by the tuberculosis bacillus.

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