ArticleBiochimica et biophysica acta. General subjects2020
BamA is required for autotransporter secretion.
Article in Biochimica et biophysica acta. General subjects, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 11 citations in OpenAlex.
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Examining Protein Translocation by β-Barrel Membrane Proteins Using Reconstituted Proteoliposomes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- TamAB is regulated by PhoPQ and functions in outer membrane homeostasis duringJournal of bacteriology · 2023Article
- Uncovering the folding mechanism of pertactin: A comparative study of isolated and vectorial folding.Biophysical journal · 2023Article
- Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021Review
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundIn Gram-negative bacteria, type Va and Vc autotransporters are proteins that contain both a secreted virulence factor (the "passenger" domain) and a β-barrel that aids its export. While it is known that the folding and insertion of the β-barrel domain utilize the β-barrel assembly machinery (BAM) complex, how the passenger domain is secreted and folded across the membrane remains to be determined. The hairpin model states that passenger domain secretion occurs independently through the fully-formed and membrane-inserted β-barrel domain via a hairpin folding intermediate. In contrast, the BamA-assisted model states that the passenger domain is secreted through a hybrid of BamA, the essential subunit of the BAM complex, and the β-barrel domain of the autotransporter.
methodsTo ascertain the models' plausibility, we have used molecular dynamics to simulate passenger domain secretion for two autotransporters, EspP and YadA.
resultsWe observed that each protein's β-barrel is unable to accommodate the secreting passenger domain in a hairpin configuration without major structural distortions. Additionally, the force required for secretion through EspP's β-barrel is more than that through the BamA β-barrel.
conclusionsSecretion of autotransporters most likely occurs through an incompletely formed β-barrel domain of the autotransporter in conjunction with BamA. GENERAL SIGNIFICANCE: Secretion of virulence factors is a process used by practically all pathogenic Gram-negative bacteria. Understanding this process is a necessary step towards limiting their infectious capacity.
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