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The well-recognized phospholipids (PLs) of  Mycobacterium tuberculosis  ( Mtb ) include several acidic species such as phosphatidylglycerol (PG), cardiolipin, phosphatidylinositol and its mannoside derivatives, in addition to a single basic species, phosphatidylethanolamine. Here we demonstrate that an additional basic PL, lysinylated PG (L-PG), is a component of the PLs of  Mtb  H37Rv and that the  lysX  gene encoding the two-domain lysyl-transferase ( mpr F)-lysyl-tRNA synthetase ( lys U) protein is responsible for L-PG production. The  Mtb lysX  mutant is sensitive to cationic antibiotics and peptides, shows increased association with lysosome-associated membrane protein–positive vesicles, and it exhibits altered membrane potential compared to wild type. A  lysX  complementing strain expressing the intact  lysX  gene, but not one expressing  mprF  alone, restored the production of L-PG and rescued the  lysX  mutant phenotypes, indicating that the expression of both proteins is required for LysX function. The  lysX  mutant also showed defective growth in mouse and guinea pig lungs and showed reduced pathology relative to wild type, indicating that LysX activity is required for full virulence. Together, our results suggest that LysX-mediated production of L-PG is necessary for the maintenance of optimal membrane integrity and for survival of the pathogen upon infection.

plos pathogens

The Two-Domain LysX Protein of Mycobacterium tuberculosis Is Required for Production of Lysinylated Phosphatidylglycerol and Resistance to Cationic Antimicrobial Peptides