Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate

• Published in: Nature chemical biology Vol. 9; no. 11; pp. 674 - 676
• Main Authors: Gouzy, Alexandre, Larrouy-Maumus, Gérald, Wu, Ting-Di, Peixoto, Antonio, Levillain, Florence, Lugo-Villarino, Geanncarlo, Guerquin-Kern, Jean-Luc, de Carvalho, Luiz Pedro Sório, Poquet, Yannick, Neyrolles, Olivier
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.11.2013; Nature Publishing Group
• Subjects: 631/326/41; 631/92/1643; 631/92/349; 692/699/255; Amino acids; Aspartic Acid - metabolism; Bacillus; Biochemical Engineering; Biochemistry; Bioorganic Chemistry; brief-communication; Cell Biology; Chemistry; Chemistry/Food Science; Colonization; Excitatory Amino Acid Transporter 1 - genetics; Excitatory Amino Acid Transporter 1 - metabolism; Immunology; Life Sciences; Molecular biology; Mutants; Mutation; Mycobacterium tuberculosis; Mycobacterium tuberculosis - metabolism; Nitrogen; Nitrogen - metabolism; Pathogens; Tuberculosis
• ISSN: 1552-4450; 1552-4469
• DOI: 10.1038/nchembio.1355

Aspartate is a primary nitrogen source for Mycobacterium tuberculosis during infection, being required for virulence after entering cells via the amino acid transporter AnsP1. 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.