期刊
NATURE
卷 496, 期 7446, 页码 508-+出版社
NATURE RESEARCH
DOI: 10.1038/nature12074
关键词
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资金
- National Institutes of Health (NIH) [AI080609, AI057141, AI105268, GM07270]
- Cystic Fibrosis Foundation [CFR565-CR07]
- National Science Foundation [PHY-084845, MCB-1151043, DGE-0718124]
- Swedish Research Council [2010-3073, 2007-8673 UCMR Linnaeus, 2006-7431 MIMS]
- Faculty of Medicine, Umea University
- University of Washington Royalty Research Fund
- Sloan Foundation
- Burroughs Wellcome Fund
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI080609, U54AI057141, R21AI105268] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007270] Funding Source: NIH RePORTER
Membranes allow the compartmentalization of biochemical processes and are therefore fundamental to life. The conservation of the cellular membrane, combined with its accessibility to secreted proteins, has made it a common target of factors mediating antagonistic interactions between diverse organisms. Here we report the discovery of a diverse superfamily of bacterial phospholipase enzymes. Within this superfamily, we defined enzymes with phospholipase A(1) and A(2) activity, which are common in host-cell-targeting bacterial toxins and the venoms of certain insects and reptiles(1,2). However, we find that the fundamental role of the superfamily is to mediate antagonistic bacterial interactions as effectors of the type VI secretion system (T6SS) translocation apparatus; accordingly, we name these proteins type VI lipase effectors. Our analyses indicate that PldA of Pseudomonas aeruginosa, a eukaryotic-like phospholipase D-3, is a member of the type VI lipase effector superfamily and the founding substrate of the haemolysin co-regulated protein secretion island II T6SS (H2-T6SS). Although previous studies have specifically implicated PldA and the H2-T6SS in pathogenesis(3-5), we uncovered a specific role for the effector and its secretory machinery in intra-and interspecies bacterial interactions. Furthermore, we find that this effector achieves its antibacterial activity by degrading phosphatidylethanolamine, the major component of bacterial membranes. The surprising finding that virulence-associated phospholipases can serve as specific antibacterial effectors suggests that interbacterial interactions are a relevant factor driving the continuing evolution of pathogenesis.
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