Rebecca Conners,1,2 Mathew McLaren,1,2 Urszula Łapińska,1,2 Kelly Sanders,1,2 M. Rhia L. Stone,3 Mark A. T. Blaskovich,3 Stefano Pagliara,1,2 Bertram Daum,1,2 Jasna Rakonjac,4 and Vicki A. M. Goldcorresponding author1,2


"1Living Systems Institute, University of Exeter, Exeter, UK
2College of Life and Environmental Sciences, Geoffrey Pope, University of Exeter, Exeter, UK
3Centre for Superbug Solutions, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland Australia
4School of Fundamental Sciences, Massey University, Palmerston North, New Zealand
Vicki A. M. Gold, Email: [email protected]"




"The Ff family of filamentous bacteriophages infect gram-negative bacteria, but do not cause lysis of their host cell. Instead, new virions are extruded via the phage-encoded pIV protein, which has homology with bacterial secretins. Here, we determine the structure of pIV from the f1 filamentous bacteriophage at 2.7 Å resolution by cryo-electron microscopy, the first near-atomic structure of a phage secretin. Fifteen f1 pIV subunits assemble to form a gated channel in the bacterial outer membrane, with associated soluble domains projecting into the periplasm. We model channel opening and propose a mechanism for phage egress. By single-cell microfluidics experiments, we demonstrate the potential for secretins such as pIV to be used as adjuvants to increase the uptake and efficacy of antibiotics in bacteria. Finally, we compare the f1 pIV structure to its homologues to reveal similarities and differences between phage and bacterial secretins.

DOI: 10.1038/s41467-021-26610-3


A fluorescence image was acquired by exposing the bacteria to the blue excitation band of a broad-spectrum LED (CoolLED pE300white, Andover, UK) at 20% of its intensity.

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The pE-300white is a popular illuminator for everyday fluorescent screening and analysis with simple operatation and individual irradiance control of each LED channel.

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Nature Communications

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