ArticleBiophysical journal2010
Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Gut Microbiota and Colonization Resistance against Bacterial Enteric Infection.Microbiology and molecular biology reviews : MMBR · 2019Review
- Identification of a pore-forming protein from sea anemoneThe journal of venomous animals and toxins including tropical diseases · 2019Article
- Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 Å resolution.Acta crystallographica. Section D, Structural biology · 2018Article
- Vibrio cholerae LeuO Links the ToxR Regulon to Expression of Lipid A Remodeling Genes.Infection and immunity · 2016Article
- Article
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
- Inspection of the engineered FhuA ΔC/Δ4L protein nanopore by polymer exclusion.Biophysical journal · 2012Article
- Practical considerations for conducting ecotoxicity test methods with manufactured nanomaterials: what have we learnt so far?Ecotoxicology (London, England) · 2012Review
- Effects of amino acid supplementation on porin expression and ToxR levels in Vibrio cholerae.Infection and immunity · 2012Article
- Positive regulation of the Vibrio cholerae porin OmpT by iron and fur.Journal of bacteriology · 2011Article
- Polymer partitioning and ion selectivity suggest asymmetrical shape for the membrane pore formed by epsilon toxin.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The trimeric OmpU and OmpT porins form large, triple-barrel hydrophilic channels in the outer membrane of the pathogen Vibrio cholerae. They have distinct pore properties, such as conductance, block by deoxycholic acid, and sensitivity to acidic pH. Their three-dimensional structures are unknown, but they share significant sequence homologies. To gain insight into the molecular basis for the distinct functional properties of these two similar porins, we carried out polymer exclusion experiments using planar lipid bilayer and patch-clamp electrophysiology. By studying the partitioning of polyethylene glycols (PEGs) of different molecular weights into each porin, we determined an effective radius of 0.55 nm and 0.43 nm for OmpU and OmpT respectively, and found an increased OmpU effective radius at acidic pH. PEGs or high buffer ionic strength promotes the appearance of single step closures in OmpU similar to the acidic-pH induced closures we documented previously. In addition, these closing events can be triggered by nonpenetrating PEGs applied asymmetrically. We believe our results support a model whereby acidic pH, high ionic strength, or exposure to PEGs stabilizes a less conductive state that corresponds to the appearance of an additional resistive element on one side of the OmpU protein and common to the three monomers.
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