期刊
MOLECULAR MICROBIOLOGY
卷 114, 期 2, 页码 308-321出版社
WILEY
DOI: 10.1111/mmi.14513
关键词
bacterial competition; cell wall degradation; peptidoglycan hydrolase; type 6 secretion system
资金
- National Natural Science Foundation of China [31622003, 31670080, 31800127, 31870060]
- China Postdoctoral Science Foundation [2018M641008]
- Postdoctoral Science Research Plan in ShaanXi Province of China [2018BSHEDZZ244]
- National Institute of Health [GM131685, GM61629]
The human pathogen Pseudomonas aeruginosa harbors three paralogous zinc proteases annotated as AmpD, AmpDh2, and AmpDh3, which turn over the cell wall and cell wall-derived muropeptides. AmpD is cytoplasmic and plays a role in the recycling of cell wall muropeptides, with a link to antibiotic resistance. AmpDh2 is a periplasmic soluble enzyme with the former anchored to the inner leaflet of the outer membrane. We document, herein, that the type VI secretion system locus II (H2-T6SS) of P. aeruginosa delivers AmpDh3 (but not AmpD or AmpDh2) to the periplasm of a prey bacterium upon contact. AmpDh3 hydrolyzes the cell wall peptidoglycan of the prey bacterium, which leads to its killing, thereby providing a growth advantage for P. aeruginosa in bacterial competition. We also document that the periplasmic protein PA0808, heretofore of unknown function, affords self-protection from lysis by AmpDh3. Cognates of the AmpDh3-PA0808 pair are widely distributed across Gram-negative bacteria. Taken together, these findings underscore the importance of their function as an evolutionary advantage and that of the H2-T6SS as the means for the manifestation of the effect.
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