Journal
SCIENCE ADVANCES
Volume 6, Issue 30, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abb5614
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Funding
- National Institute of Allergy and Infectious Diseases (NIAID) [R21 AI137188]
- Wellcome Trust [101824/Z/13/Z]
- U.K. Medical Research Council within the Antimicrobial Resistance Cross-Council Initiative collaborative grant [MR/N002679/1]
- Swedish Research Council (VR)
- Knut and Alice Wallenberg Foundation (KAW)
- Laboratory of Molecular Infection Medicine Sweden (MIMS)
- Kempe Foundation
- NIAID [R01 AI101171]
- NIH [GM127331]
- NSF [DGE-1745038]
- German Research Foundation (DFG) [EB-285-2/2]
- MRC [MR/N002679/1] Funding Source: UKRI
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Peptidoglycan (PG) is essential in most bacteria. Thus, it is often targeted by various assaults, including interbacterial attacks via the type VI secretion system (T6SS). Here, we report that the Gram-negative bacterium Acinetobacter baumannii strain ATCC 17978 produces, secretes, and incorporates the noncanonical D-amino acid D-lysine into its PG during stationary phase. We show that PG editing increases the competitiveness of A. baumannii during bacterial warfare by providing immunity against peptidoglycan-targeting T6SS effectors from various bacterial competitors. In contrast, we found that D-Lys production is detrimental to pathogenesis due, at least in part, to the activity of the human enzyme d-amino acid oxidase (DAO), which degrades D-Lys producing H2O2 toxic to bacteria. Phylogenetic analyses indicate that the last common ancestor of A. baumannii had the ability to produce D-Lys. However, this trait was independently lost multiple times, likely reflecting the evolution of A. baumannii as a human pathogen.
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