Type VI secretion delivers bacteriolytic effectors to target cells

Alistair B. Russell, Rachel D. Hood, Nhat Khai Bui, Michele LeRoux, Waldemar Vollmer and Joseph D. Mougous ()
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Alistair B. Russell: University of Washington
Rachel D. Hood: University of Washington
Nhat Khai Bui: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK
Michele LeRoux: Molecular and Cellular Biology Program, University of Washington
Waldemar Vollmer: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK
Joseph D. Mougous: University of Washington

Nature, 2011, vol. 475, issue 7356, 343-347

Abstract: Abstract Peptidoglycan is the major structural constituent of the bacterial cell wall, forming a meshwork outside the cytoplasmic membrane that maintains cell shape and prevents lysis. In Gram-negative bacteria, peptidoglycan is located in the periplasm, where it is protected from exogenous lytic enzymes by the outer membrane. Here we show that the type VI secretion system of Pseudomonas aeruginosa breaches this barrier to deliver two effector proteins, Tse1 and Tse3, to the periplasm of recipient cells. In this compartment, the effectors hydrolyse peptidoglycan, thereby providing a fitness advantage for P. aeruginosa cells in competition with other bacteria. To protect itself from lysis by Tse1 and Tse3, P. aeruginosa uses specific periplasmically localized immunity proteins. The requirement for these immunity proteins depends on intercellular self-intoxication through an active type VI secretion system, indicating a mechanism for export whereby effectors do not access donor cell periplasm in transit.

Date: 2011
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DOI: 10.1038/nature10244

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