ArticleJournal of bacteriology2008
Oms38 is the first identified pore-forming protein in the outer membrane of relapsing fever spirochetes.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Experimental evidence rules out mosquitoes as vectors of Lyme disease.Parasites & vectors · 2025Article
- Development and validation of systems for genetic manipulation of the Old World tick-borne relapsing fever spirochete, Borrelia duttonii.PLoS neglected tropical diseases · 2024Article
- Article
- OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins.Frontiers in bioinformatics · 2021Article
- Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.BMC microbiology · 2016Article
- Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin.The Journal of biological chemistry · 2014Article
- Article
- Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification.The Journal of biological chemistry · 2011Article
- Alzheimer's disease - a neurospirochetosis. Analysis of the evidence following Koch's and Hill's criteria.Journal of neuroinflammation · 2011Review
- Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete.Journal of bacteriology · 2009Article
- A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans.PloS one · 2009Article
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Authors and funding
11 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Relapsing fever is a worldwide, endemic disease caused by several spirochetal species belonging to the genus Borrelia. During the recurring fever peaks, borreliae proliferate remarkably quickly compared to the slow dissemination of Lyme disease Borrelia and therefore require efficient nutrient uptake from the blood of their hosts. This study describes the identification and characterization of the first relapsing fever porin, which is present in the outer membranes of B. duttonii, B. hermsii, B. recurrentis, and B. turicatae. The pore-forming protein was purified by hydroxyapatite chromatography and designated Oms38, for outer membrane-spanning protein of 38 kDa. Biophysical characterization of Oms38 was done by using the black lipid bilayer method, demonstrating that Oms38 forms small, water-filled channels of 80 pS in 1 M KCl that did not exhibit voltage-dependent closure. The Oms38 channel is slightly selective for anions and shows a ratio of permeability for cations over anions of 0.41 in KCl. Analysis of the deduced amino acid sequences demonstrated that Oms38 contains an N-terminal signal sequence which is processed under in vivo conditions. Oms38 is highly conserved within the four studied relapsing fever species, sharing an overall amino acid identity of 58% and with a strong indication for the presence of amphipathic beta-sheets.
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