Bacteriocin biophysics: From protein–protein interaction models to navigators of the bacterial cell envelope

Bacteriocins are toxins deployed by bacteria to kill their competitors. Here, I reflect on my laboratory's work on protein bacteriocins and their immunity proteins from Gram-negative bacteria. We uncovered the structural and biophysical principles that underpin the 10-log stability range of protective immunity proteins for cytotoxic nuclease bacteriocins. We went on to elucidate how bacteriocins that kill Escherichia coli, Pseudomonas aeruginosa, and Klebsiella pneumoniae subvert outer membrane proteins and periplasmic energy transduction systems to drive their import. We leveraged our understanding of bacteriocin structure and function to probe the nature of the bacterial outer membrane. These studies revealed the outer membrane of E. coli to be an asymmetric proteolipid membrane, not an asymmetric lipid membrane as has been accepted dogma for the last 50 years. I contextualize the work with background on my career, collaborations, and academic leadership roles that influenced my development as a scientist.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2026-01-23
DOI
https://doi.org/10.1016/j.jbc.2026.111185
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00

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article

Bacteriocin biophysics: From protein–protein interaction models to navigators of the bacterial cell envelope

Colin Kleanthous
Journal of Biological Chemistry
Bacterial Genetics and Biotechnology
article

Bacteriocin biophysics: From protein–protein interaction models to navigators of the bacterial cell envelope

Colin Kleanthous
article en

Abstract

Bacteriocins are toxins deployed by bacteria to kill their competitors. Here, I reflect on my laboratory's work on protein bacteriocins and their immunity proteins from Gram-negative bacteria. We uncovered the structural and biophysical principles that underpin the 10-log stability range of protective immunity proteins for cytotoxic nuclease bacteriocins. We went on to elucidate how bacteriocins that kill Escherichia coli, Pseudomonas aeruginosa, and Klebsiella pneumoniae subvert outer membrane proteins and periplasmic energy transduction systems to drive their import. We leveraged our understanding of bacteriocin structure and function to probe the nature of the bacterial outer membrane. These studies revealed the outer membrane of E. coli to be an asymmetric proteolipid membrane, not an asymmetric lipid membrane as has been accepted dogma for the last 50 years. I contextualize the work with background on my career, collaborations, and academic leadership roles that influenced my development as a scientist.

Journal of Biological ChemistryVol. 302(3)
University of Oxford (GB)
Wellcome Trust, Biotechnology and Biological Sciences Research Council
Affordable and clean energy
Openalex Percentile: Top 75%
Bacterial Genetics and Biotechnology
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Bacteriocin biophysics: From protein–protein interaction models to navigators of the bacterial cell envelope — Colin Kleanthous · Journal of Biological Chemistry (2026) | TGRS Research Map | TGRS