Elimination of channel-forming activity by insertional inactivation of the p66 gene in Borrelia burgdorferi

FEMS Microbiol Lett. 2007 Jan;266(2):241-9. doi: 10.1111/j.1574-6968.2006.00529.x.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology
  • Borrelia burgdorferi / genetics*
  • Borrelia burgdorferi / metabolism
  • Genetic Complementation Test
  • Immunoblotting
  • Ion Channels / genetics
  • Ion Channels / metabolism
  • Ion Channels / physiology
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology
  • Mutagenesis, Insertional
  • Mutation
  • Porins / genetics*
  • Porins / metabolism
  • Porins / physiology

Substances

  • Bacterial Proteins
  • Ion Channels
  • Membrane Proteins
  • Oms66 protein, Borrelia
  • Porins