Tn-Seq reveals hidden complexity in the utilization of host-derived glutathione in Francisella tularensis
Autoři:
Kathryn M. Ramsey aff001; Hannah E. Ledvina aff003; Tenayaann M. Tresko aff003; Jamie M. Wandzilak aff002; Catherine A. Tower aff003; Thomas Tallo aff001; Caroline E. Schramm aff004; S. Brook Peterson aff003; Shawn J. Skerrett aff004; Joseph D. Mougous aff003; Simon L. Dove aff001
Působiště autorů:
Division of Infectious Diseases, Boston Children’s Hospital, Harvard Medical School, Boston, Massachusetts, United States of America
aff001; Departments of Cell and Molecular Biology and Biomedical and Pharmaceutical Sciences, University of Rhode Island, Kingston, Rhode Island, United States of America
aff002; Department of Microbiology, University of Washington School of Medicine, Seattle, Washington, United States of America
aff003; Division of Pulmonary, Critical Care and Sleep Medicine, Harborview Medical Center, University of Washington, Seattle, Washington, United States of America
aff004; Howard Hughes Medical Institute, University of Washington, Seattle, Washington, United States of America
aff005
Vyšlo v časopise:
Tn-Seq reveals hidden complexity in the utilization of host-derived glutathione in Francisella tularensis. PLoS Pathog 16(6): e32767. doi:10.1371/journal.ppat.1008566
Kategorie:
Research Article
doi:
https://doi.org/10.1371/journal.ppat.1008566
Souhrn
Host-derived glutathione (GSH) is an essential source of cysteine for the intracellular pathogen Francisella tularensis. In a comprehensive transposon insertion sequencing screen, we identified several F. tularensis genes that play central and previously unappreciated roles in the utilization of GSH during the growth of the bacterium in macrophages. We show that one of these, a gene we named dptA, encodes a proton-dependent oligopeptide transporter that enables growth of the organism on the dipeptide Cys-Gly, a key breakdown product of GSH generated by the enzyme γ-glutamyltranspeptidase (GGT). Although GGT was thought to be the principal enzyme involved in GSH breakdown in F. tularensis, our screen identified a second enzyme, referred to as ChaC, that is also involved in the utilization of exogenous GSH. However, unlike GGT and DptA, we show that the importance of ChaC in supporting intramacrophage growth extends beyond cysteine acquisition. Taken together, our findings provide a compendium of F. tularensis genes required for intracellular growth and identify new players in the metabolism of GSH that could be attractive targets for therapeutic intervention.
Klíčová slova:
Cysteine – Cytoplasm – Francisella – Francisella tularensis – Genetic screens – Library screening – Macrophages – Transposable elements
Zdroje
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