ArticleInfection and immunity1997
The Oms66 (p66) protein is a Borrelia burgdorferi porin.
Article in Infection and immunity, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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74 citing papers in PubMed, 118 citations in OpenAlex.
- UrinaryJournal of cellular immunology · 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
- P66 is a bacterial mimic of CD47 that binds the anti-phagocytic receptor SIRPα and facilitates macrophage evasion bybioRxiv : the preprint server for biology · 2024Article
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- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes.Pathogens and disease · 2023Article
- Allelic Variants ofMicroorganisms · 2022Article
- Transmission Cycle of Tick-Borne Infections and Co-Infections, Animal Models and Diseases.Pathogens (Basel, Switzerland) · 2022Review
- Identification of amino acid domains ofFrontiers in cellular and infection microbiology · 2022Article
- Pathogenesis of Relapsing Fever.Current issues in molecular biology · 2021Review
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- A Novel Laminin-Binding Protein Mediates Microbial-Endothelial Cell Interactions and Facilitates Dissemination of Lyme Disease Pathogens.The Journal of infectious diseases · 2020Article
- Membrane directed expression in Escherichia coli of BBA57 and other virulence factors from the Lyme disease agent Borrelia burgdorferi.Scientific reports · 2019Article
- Delineating Surface Epitopes of Lyme Disease Pathogen Targeted by Highly Protective Antibodies of New Zealand White Rabbits.Infection and immunity · 2019Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- A bite so sweet: the glycobiology interface of tick-host-pathogen interactions.Parasites & vectors · 2018Review
- HtrA of Borrelia burgdorferi Leads to Decreased Swarm Motility and Decreased Production of Pyruvate.mBio · 2018Article
- Characterization of Stress and Innate Immunity Resistance of Wild-Type and ΔInfection and immunity · 2018Article
14 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
Abstract
In this study we report the purification and characterization of a 66-kDa protein, designated Oms66, for outer membrane-spanning 66-kDa protein, that functions as a porin in the outer membrane (OM) of Borrelia burgdorferi. Oms66 was purified by fast-performance liquid chromatography and exhibited an average single-channel conductance of 9.62 +/- 0.37 nS in 1 M KCl, as evidenced by 581 individual insertional events in planar lipid bilayers. Electrophysiological characterization indicated that Oms66 was virtually nonselective between cations and anions and exhibited voltage-dependent closure with multiple substates. The amino acid sequence of tryptic peptides derived from purified Oms66 was identical to the deduced amino acid sequence of p66, a previously described surface-exposed protein of B. burgdorferi. Purified Oms66 was recognized by antiserum specific for p66 and serum from rabbits immune to challenge with virulent B. burgdorferi, indicating that p66 and Oms66 were identical proteins and that Oms66/p66 is an immunogenic protein in infected rabbits. In a methodology that reduces liposomal trapping and nonspecific interactions, native Oms66 was incorporated into liposomes, confirming that Oms66 is an outer membrane-spanning protein. Proteoliposomes containing Oms66 exhibited porin activity nearly identical to that of native, purified Oms66, indicating that reconstituted Oms66 retained native conformation. The use of proteoliposomes reconstituted with Oms66 and other Oms proteins provides an experimental system for determinating the relationship between conformation, protection, and biological function of these molecules.
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