ArticleJournal of bacteriology2014
Bacterial secretins form constitutively open pores akin to general porins.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Secretin-interacting plug proteins prevent antibiotic influx during type IV pilus assembly in Pseudomonas aeruginosa.Nature communications · 2026Article
- Secretins of type-two secretion systems are necessary for exopolymeric slime secretion in cyanobacteria and myxobacteria.Nature communications · 2025Article
- Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane.Microbial cell (Graz, Austria) · 2019Article
- Characterization of the Vibrio cholerae Phage Shock Protein Response.Journal of bacteriology · 2019Article
- Controlling Secretion in Artificial Cells with a Membrane AND Gate.ACS synthetic biology · 2019Article
- Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin.Nature communications · 2018Article
- Article
- Glyconanomaterials for Combating Bacterial Infections.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins called secretins form large multimeric complexes that are essential for macromolecular transit across the outer membrane of Gram-negative bacteria. Evidence suggests that the channels formed by some secretin complexes are not tightly closed, but their permeability properties have not been well characterized. Here, we used cell-free synthesis coupled with spontaneous insertion into liposomes to investigate the permeability of the secretin PulD. Leakage assays using preloaded liposomes indicated that PulD allows the efflux of small fluorescent molecules with a permeation cutoff similar to that of general porins. Other secretins were also found to form similar pores. To define the polypeptide region involved in determining the pore size, we analyzed a collection of PulD variants and studied the roles of gates 1 and 2, which were previously reported to affect the pore size of filamentous phage f1 secretin pIV, in assembly and pore formation. Liposome leakage and a novel in vivo assay showed that replacement of the conserved proline residue at position 443 in PulD by leucine increased the apparent size of the pore. The in vitro approach described here could be used to study the pore properties of membrane proteins whose production in vivo is toxic.
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Registered trials
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