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

ABSTRACT: OmpA, a predominant outer membrane protein (OMP) in Gram-negative bacteria, plays a crucial role in maintaining the integrity and functionality of the bacterial outer membrane (OM). Despite its significance in virulence, adhesion, and OM stability, the specific role of OmpA has remained unclear since its discovery 50 years ago. In this study, we demonstrate that OmpA organizes the OMP lattice and mechanically connects it to the cell wall. Using atomic force microscopy, simulations, and microfluidics, we show that while the β-barrel domain of OmpA is essential for maintaining the permeability barrier, both the β-barrel and cell wall-binding domains are necessary to enhance the cell envelope's strength. We propose that OmpA integrates the compressive properties of the OMP lattice with the tensile strength of the cell wall, forming a mechanically robust composite that enhances overall envelope integrity. This coupling likely underpins the ability of the entire envelope to function as a cohesive and resilient structure, critical for the survival and pathogenicity of Gram-negative bacteria.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Escherichia Coli

SUBMITTER: Alex Johnson

LAB HEAD: Martin Wühr

PROVIDER: PXD054033 | Pride | 2024-11-20

REPOSITORIES: Pride

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			Action	DRS
	TGR_16668.pep.xml	Pepxml
	TGR_16668.raw	Raw
	checksum.txt	Txt

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