Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis

Robert S. Jansen, Lungelo Mandyoli, Ryan Hughes, Shoko Wakabayashi, Jessica T. Pinkham, Bruna Selbach, Kristine M. Guinn, Eric J. Rubin, James C. Sacchettini () and Kyu Y. Rhee ()
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Robert S. Jansen: Division of Infectious Diseases, Department of Medicine, Weill Cornell Medical College
Lungelo Mandyoli: Department of Biochemistry and Biophysics, Texas A&M University
Ryan Hughes: Department of Biochemistry and Biophysics, Texas A&M University
Shoko Wakabayashi: Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health
Jessica T. Pinkham: Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health
Bruna Selbach: Division of Infectious Diseases, Department of Medicine, Weill Cornell Medical College
Kristine M. Guinn: Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health
Eric J. Rubin: Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health
James C. Sacchettini: Department of Biochemistry and Biophysics, Texas A&M University
Kyu Y. Rhee: Division of Infectious Diseases, Department of Medicine, Weill Cornell Medical College

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract Gene rv3722c of Mycobacterium tuberculosis is essential for in vitro growth, and encodes a putative pyridoxal phosphate-binding protein of unknown function. Here we use metabolomic, genetic and structural approaches to show that Rv3722c is the primary aspartate aminotransferase of M. tuberculosis, and mediates an essential but underrecognized role in metabolism: nitrogen distribution. Rv3722c deficiency leads to virulence attenuation in macrophages and mice. Our results identify aspartate biosynthesis and nitrogen distribution as potential species-selective drug targets in M. tuberculosis.

Date: 2020
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DOI: 10.1038/s41467-020-15876-8

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