ArticleJournal of bacteriology2002
Elimination of channel-forming activity by insertional inactivation of the p13 gene in Borrelia burgdorferi.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Identification of Surface Epitopes Associated with Protection against Highly Immune-Evasive VlsE-Expressing Lyme Disease Spirochetes.Infection and immunity · 2018Article
- Outer Membrane Proteins BB0405 and BB0406 Are Immunogenic, but Only BB0405 Is Required for Borrelia burgdorferi Infection.Infection and immunity · 2017Article
- Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.BMC microbiology · 2016Article
- A Borrelia burgdorferi Surface-Exposed Transmembrane Protein Lacking Detectable Immune Responses Supports Pathogen Persistence and Constitutes a Vaccine Target.The Journal of infectious diseases · 2016Article
- The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning β-barrel.Bioscience reports · 2015Article
- Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin.The Journal of biological chemistry · 2014Article
- Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.Journal of bacteriology · 2014Article
- The role of Borrelia burgdorferi outer surface proteins.FEMS immunology and medical microbiology · 2012Review
- Article
- Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing.Journal of bacteriology · 2011Article
- A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans.PloS one · 2009Article
- Oms38 is the first identified pore-forming protein in the outer membrane of relapsing fever spirochetes.Journal of bacteriology · 2008Article
- An RND-type efflux system in Borrelia burgdorferi is involved in virulence and resistance to antimicrobial compounds.PLoS pathogens · 2008Article
- Borrelia burgdorferi BBA74, a periplasmic protein associated with the outer membrane, lacks porin-like properties.Journal of bacteriology · 2007Article
- The BBA01 protein, a member of paralog family 48 from Borrelia burgdorferi, is potentially interchangeable with the channel-forming protein P13.Journal of bacteriology · 2006Article
- Borrelia burgdorferi lacking BBK32, a fibronectin-binding protein, retains full pathogenicity.Infection and immunity · 2006Article
- Comparative transcriptional profiling of Borrelia burgdorferi clinical isolates differing in capacities for hematogenous dissemination.Infection and immunity · 2005Article
- The etiological agent of Lyme disease, Borrelia burgdorferi, appears to contain only a few small RNA molecules.Journal of bacteriology · 2004Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
P13 is a chromosomally encoded 13-kDa integral outer membrane protein of the Lyme disease agent, Borrelia burgdorferi. The aim of this study was to investigate the function of the P13 protein. Here, we inactivated the p13 gene by targeted mutagenesis and investigated the porin activities of outer membrane proteins by using lipid bilayer experiments. Channel-forming activity was lost in the p13 mutant compared to wild-type B. burgdorferi, indicating that P13 may function as a porin. We purified native P13 to homogeneity by fast performance liquid chromatography and demonstrated that pure P13 has channel-forming activity with a single-channel conductance in 1 M KCl of 3.5 nS, the same as the porin activity that was lost in the p13 mutant. Further characterization of the channel formed by P13 suggested that it is cation selective and voltage independent. In addition, no major physiological effects of the inactivated p13 gene could be detected under normal growth conditions. The inactivation of p13 is the first reported inactivation of a gene encoding an integral outer membrane protein in B. burgdorferi. Here, we describe both genetic and biophysical experiments indicating that P13 in B. burgdorferi is an outer membrane protein with porin activity.
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