title: Elimination of channel-forming activity by insertional inactivation of the p66 gene in Borrelia burgdorferi.
abstract: P66 is a chromosomally encoded 66-kDa integral outer membrane protein of the Lyme disease agent Borrelia burgdorferi exhibiting channel-forming activity. Herein, we inactivated and subsequently complemented the p66 gene in the B31-A (WT) strain. The P66 protein was also inactivated in two other channel-forming protein mutant strains, P13-18 (Deltap13) and Deltabba01, and then compared with the channel-forming activities of wild-type and various p66 mutant strains. We further investigated the ion-selectivity of native, purified P66. In conclusion, we show that the porin activity of P66 is eliminated by insertional inactivation and that this activity can be rescued by gene complementation.
authors.affiliation: Department of Molecular Biology, Umeå University, Sweden.
authors.forename: Marija
authors.initials: M
authors.lastname: Pinne
authors.forename: Marcus
authors.initials: M
authors.lastname: Thein
authors.forename: Katrin
authors.initials: K
authors.lastname: Denker
authors.forename: Roland
authors.initials: R
authors.lastname: Benz
authors.forename: Jenifer
authors.initials: J
authors.lastname: Coburn
authors.forename: Sven
authors.initials: S
authors.lastname: Bergström
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D025065:Borrelia burgdorferi / Q000235:genetics* / Q000378:metabolism; D005816:Genetic Complementation Test; D015151:Immunoblotting; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D016254:Mutagenesis, Insertional; D009154:Mutation; D018272:Porins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D007473:Ion Channels; D008565:Membrane Proteins; C107893:Oms66 protein, Borrelia; D018272:Porins