Benn, Georgina;
Borrelli, Carolina;
Prakaash, Dheeraj;
Johnson, Alex NT;
Fideli, Vincent A;
Starr, Tahj;
Fitzmaurice, Dylan;
... Silhavy, Thomas J; + view all
(2024)
OmpA controls order in the outer membrane and shares the mechanical load.
Proceedings of the National Academy of Sciences (PNAS)
, 121
(50)
, Article e2416426121. 10.1073/pnas.2416426121.
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Abstract
OmpA, a predominant outer membrane (OM) protein in Escherichia coli, affects virulence, adhesion, and bacterial OM integrity. However, despite more than 50 y of research, the molecular basis for the role of OmpA has remained elusive. In this study, we demonstrate that OmpA organizes the OM protein lattice and mechanically connects it to the cell wall (CW). Using gene fusions, atomic force microscopy, simulations, and microfluidics, we show that the β-barrel domain of OmpA is critical for maintaining the permeability barrier, but both the β-barrel and CW-binding domains are necessary to enhance the cell envelope's strength. OmpA integrates the compressive properties of the OM protein lattice with the tensile strength of the CW, forming a mechanically robust composite that increases overall integrity. This coupling likely underpins the ability of the entire envelope to function as a cohesive, resilient structure, critical for the survival of bacteria.
| Type: | Article |
|---|---|
| Title: | OmpA controls order in the outer membrane and shares the mechanical load |
| Location: | United States |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1073/pnas.2416426121 |
| Publisher version: | https://doi.org/10.1073/pnas.2416426121 |
| Language: | English |
| Additional information: | This work is licensed under a Creative Commons License. The images or other third-party material in this article are included in the Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| Keywords: | Science & Technology, Multidisciplinary Sciences, Science & Technology - Other Topics, outer membrane, atomic force microscopy, membrane biophysics, membrane organisation, BACTERIAL-CELL WALL, ESCHERICHIA-COLI, MOLECULAR-DYNAMICS, PROTEIN, ENVELOPE, QUANTIFICATION, PEPTIDOGLYCAN, PROTEOMICS |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10205234 |
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