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Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate
Here we identify the amino acid transporter AnsP1 as the unique aspartate importer in the human pathogen Mycobacterium tuberculosis. Metabolomic analysis of a mutant inactivated in AnsP1 revealed the transporter is essential for M. tuberculosis to assimilate nitrogen from aspartate. Virulence of the...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856356/ https://www.ncbi.nlm.nih.gov/pubmed/24077180 http://dx.doi.org/10.1038/nchembio.1355 |
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author | Gouzy, Alexandre Larrouy-Maumus, Gérald Wu, Ting-Di Peixoto, Antonio Levillain, Florence Lugo-Villarino, Geanncarlo Gerquin-Kern, Jean-Luc de Carvalho, Luiz Pedro Sório Poquet, Yannick Neyrolles, Olivier |
author_facet | Gouzy, Alexandre Larrouy-Maumus, Gérald Wu, Ting-Di Peixoto, Antonio Levillain, Florence Lugo-Villarino, Geanncarlo Gerquin-Kern, Jean-Luc de Carvalho, Luiz Pedro Sório Poquet, Yannick Neyrolles, Olivier |
author_sort | Gouzy, Alexandre |
collection | PubMed |
description | Here we identify the amino acid transporter AnsP1 as the unique aspartate importer in the human pathogen Mycobacterium tuberculosis. Metabolomic analysis of a mutant inactivated in AnsP1 revealed the transporter is essential for M. tuberculosis to assimilate nitrogen from aspartate. Virulence of the AnsP1 mutant is impaired in vivo, revealing aspartate is a primary nitrogen source required for host colonization by the tuberculosis bacillus. |
format | Online Article Text |
id | pubmed-3856356 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-38563562014-05-01 Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate Gouzy, Alexandre Larrouy-Maumus, Gérald Wu, Ting-Di Peixoto, Antonio Levillain, Florence Lugo-Villarino, Geanncarlo Gerquin-Kern, Jean-Luc de Carvalho, Luiz Pedro Sório Poquet, Yannick Neyrolles, Olivier Nat Chem Biol Article Here we identify the amino acid transporter AnsP1 as the unique aspartate importer in the human pathogen Mycobacterium tuberculosis. Metabolomic analysis of a mutant inactivated in AnsP1 revealed the transporter is essential for M. tuberculosis to assimilate nitrogen from aspartate. Virulence of the AnsP1 mutant is impaired in vivo, revealing aspartate is a primary nitrogen source required for host colonization by the tuberculosis bacillus. 2013-09-29 2013-11 /pmc/articles/PMC3856356/ /pubmed/24077180 http://dx.doi.org/10.1038/nchembio.1355 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Gouzy, Alexandre Larrouy-Maumus, Gérald Wu, Ting-Di Peixoto, Antonio Levillain, Florence Lugo-Villarino, Geanncarlo Gerquin-Kern, Jean-Luc de Carvalho, Luiz Pedro Sório Poquet, Yannick Neyrolles, Olivier Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title | Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title_full | Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title_fullStr | Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title_full_unstemmed | Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title_short | Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
title_sort | mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856356/ https://www.ncbi.nlm.nih.gov/pubmed/24077180 http://dx.doi.org/10.1038/nchembio.1355 |
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