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Pyocin s5 import into Pseudomonas aeruginosa reveals a generic mode of bacteriocin transport

DOI: 10.1128/mBio.03230-19 DOI Help

Authors: Hannah M. Behrens (University of Oxford) , Edward D. Lowe (University of Oxford) , Joseph Gault (University of Oxford) , Nicholas G. Housden (University of Oxford) , Renata Kaminska (University of Oxford) , T. Moritz Weber (Heinrich Heine University Düsseldorf, Forschungszentrum Jülich) , Catriona M. A. Thompson (University of Glasgow) , Gaëtan L. A. Mislin (UMR 7242, Biotechnologie et Signalisation Cellulaire, ESBS) , Isabelle J. Schalk (UMR 7242, Biotechnologie et Signalisation Cellulaire, ESBS) , Daniel Walker (University of Glasgow) , Carol V. Robinson (University of Oxford) , Colin Kleanthous (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Mbio , VOL 11

State: Published (Approved)
Published: April 2020
Diamond Proposal Number(s): 23459

Open Access Open Access

Abstract: Pyocin S5 (PyoS5) is a potent protein bacteriocin that eradicates the human pathogen Pseudomonas aeruginosa in animal infection models, but its import mechanism is poorly understood. Here, using crystallography, biophysical and biochemical analyses, and live-cell imaging, we define the entry process of PyoS5 and reveal links to the transport mechanisms of other bacteriocins. In addition to its C-terminal pore-forming domain, elongated PyoS5 comprises two novel tandemly repeated kinked 3-helix bundle domains that structure-based alignments identify as key import domains in other pyocins. The central domain binds the lipid-bound common polysaccharide antigen, allowing the pyocin to accumulate on the cell surface. The N-terminal domain binds the ferric pyochelin transporter FptA while its associated disordered region binds the inner membrane protein TonB1, which together drive import of the bacteriocin across the outer membrane. Finally, we identify the minimal requirements for sensitizing Escherichia coli toward PyoS5, as well as other pyocins, and suggest that a generic pathway likely underpins the import of all TonB-dependent bacteriocins across the outer membrane of Gram-negative bacteria.

Journal Keywords: membrane; pyocin; transport

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Chemistry, Medicine

Instruments: B21-High Throughput SAXS

Added On: 02/04/2020 12:02


Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Biochemistry Chemistry Structural biology Biophysics Drug Discovery Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)