OmpA controls order in the outer membrane and shares the mechanical load

OmpA, a predominant outer membrane (OM) protein in <i>Escherichia coli</i>, 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.

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Institutions

Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2024-12-04
DOI
https://doi.org/10.1073/pnas.2416426121
Citations
20
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
11.01

Funders

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article

OmpA controls order in the outer membrane and shares the mechanical load

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20 citations
Proceedings of the National Academy of Sciences
Bacterial Genetics and Biotechnology
11.01
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OmpA controls order in the outer membrane and shares the mechanical load

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article en
20 citations

Abstract

OmpA, a predominant outer membrane (OM) protein in <i>Escherichia coli</i>, 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.

Proceedings of the National Academy of SciencesVol. 121(50)
Princeton University (US), London Centre for Nanotechnology (GB), University of Oxford (GB), University College London (GB), Imperial College London (GB), New York University (US)
National Science Foundation, Wellcome Trust, Science Foundation Ireland, Directorate for Biological Sciences, Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, National Institute of General Medical Sciences
Openalex Percentile: Top 1%
Bacterial Genetics and Biotechnology
11.01
DOIOpen Access PDFOpenAlex
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