Characterization of Phosphopantetheinyl Hydrolase from Mycobacterium tuberculosis

• DOI: 10.1128/spectrum.00928-21
• Publication Date: 2021-09-22T18:37:16Z
• Authors: Shilpika Pandey; Amrita Singh; Guangli Yang; Felipe B. d’Andrea; Xiuju Jiang; Travis E. Hartman; John W. Mosior; Ronnie Bourland; Ben Gold; Julia Roberts; Annie Geiger; Su Tang; Kyu Rhee; Ouathek Ouerfelli; James C. Sacchettini; Carl F. Nathan; Kristin Burns-Huang
• Keywords: Microbiology; metallophosphodiesterase; Mice; 03 medical and health sciences; Bacterial Proteins; Cell Wall; Animals; Humans; Tuberculosis; CoA salvage; phosphopantetheinyl hydrolase; 0303 health sciences; Virulence; Phosphoric Diester Hydrolases; Mycobacterium tuberculosis; Lipids; QR1-502; 3. Good health; Mice, Inbred C57BL; carrier protein; Pantetheine; dephosphopantetheinylation; Female; Protein Processing, Post-Translational; Research Article

Tuberculosis (TB), caused by Mycobacterium tuberculosis , was the leading cause of death from an infectious disease before COVID, yet the in vivo essentiality and function of many of the protein-encoding genes expressed by M. tuberculosis are not known. We biochemically characterize M. tuberculosis ’s phosphopantetheinyl hydrolase, PptH, a protein unique to mycobacteria that removes an essential posttranslational modification on proteins involved in synthesis of lipids important for the bacterium’s cell wall and virulence.