ArticleJournal of bacteriology1996
Porins of Vibrio cholerae: purification and characterization of OmpU.
Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 116 citations in OpenAlex.
- Modular small RNA drives the emergence of virulence traits and environmental trade-offs in Vibrio cholerae.Nature communications · 2026Article
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- Allelic diversity uncovers protein domains contributing to the emergence of antimicrobial resistance.PLoS genetics · 2023Article
- Effects of NaCl Concentration on the Behavior ofFoods (Basel, Switzerland) · 2022Article
- Identification of Potent Natural Resource Small Molecule Inhibitor to ControlMolecules (Basel, Switzerland) · 2021Article
- Vibrio cholerae TolC Is Required for Expression of the ToxR Regulon.Infection and immunity · 2021Article
- Single-channel properties, sugar specificity, and role of chitoporin in adaptive survival ofThe Journal of biological chemistry · 2020Article
- Outer Membrane Vesiculation Facilitates Surface Exchange and In Vivo Adaptation of Vibrio cholerae.Cell host & microbe · 2020Article
- Synthesis, Characterization, Antibacterial Activity, and Computer-Aided Design of Novel Quinazolin-2,4-dione Derivatives as Potential Inhibitors AgainstEvolutionary bioinformatics online · 2020Article
- Ambient pH Alters the Protein Content of Outer Membrane Vesicles, Driving Host Development in a Beneficial Symbiosis.Journal of bacteriology · 2019Article
- Intermembrane transport: Glycerophospholipid homeostasis of the Gram-negative cell envelope.Proceedings of the National Academy of Sciences of the United States of America · 2019Review
- Structural basis for chitin acquisition by marine Vibrio species.Nature communications · 2018Article
- Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 Å resolution.Acta crystallographica. Section D, Structural biology · 2018Article
- Growth arrest and a persister state enable resistance to osmotic shock and facilitate dissemination of Vibrio cholerae.The ISME journal · 2017Article
- Vibrio cholerae Porin OmpU Induces Caspase-independent Programmed Cell Death upon Translocation to the Host Cell Mitochondria.The Journal of biological chemistry · 2015Article
- The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Clinical microbiology reviews · 2015Review
- Role of 6-gingerol in reduction of cholera toxin activity in vitro and in vivo.Antimicrobial agents and chemotherapy · 2013Article
- Article
- Structural and functional importance of outer membrane proteins in Vibrio cholerae flagellum.Journal of microbiology (Seoul, Korea) · 2012Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three outer membrane proteins with molecular masses of 40, 38, and 27 kDa of the hypertoxinogenic strain 569B of Vibrio cholerae have been purified to homogeneity. The synthesis of all the three proteins is regulated by the osmolarity of the growth medium. The pore-forming ability of the 40-kDa protein, OmpT, and the 38-kDa protein, OmpU, has been demonstrated by using liposomes, in which these proteins were embedded. The 27-kDa protein, OmpX, though osmoregulated, is not a porin. OmpU constitutes 30% of the total outer membrane protein when grown in the presence of 1.0% NaCl in the growth medium and 60% in the absence of NaCl. OmpU is an acidic protein and is a homotrimer of 38-kDa monomeric units. Its secondary structure contains predominantly a beta-sheet, and three to four Ca2+ ions are associated with each monomeric unit. Removal of Ca2+ irreversibly disrupts the structure and pore-forming ability of the protein. The pore size of OmpU is 1.6 nm, and the specific activity of the OmpU channel is two- to threefold higher than that of Escherichia coli porin OmpF, synthesis of which resembles that of OmpU with respect to the osmolarity of the growth medium. The pore size of OmpT, which is analogous to OmpC of E. coli, is smaller than that of OmpU. Southern blot hybridization of V. cholerae genomic DNA digested with several restriction endonucleases with nick-translated E. coli ompF as the probe revealed no nucleotide sequence homology between the ompU and ompF genes. OmpU is also not antigenically related to OmpF. Anti-OmpF antiserum, however, cross-reacted with the 45-kDa V. cholerae outer membrane protein, OmpS, the synthesis of which is regulated by the presence of maltose in the growth medium. OmpU hemagglutinated with rabbit and human blood. This toxR-regulated protein is one of the possible virulence determinants in V. cholerae (V. L. Miller and J. J. Mekalanos, J. Bacteriol. 170:2575-2583, 1988).
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