Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin.

ABSTRACT: P13 is one of the major outer membrane proteins of Borrelia burgdorferi. Previous studies described P13 as a porin. In the present study some structure and function aspects of P13 were studied. P13 showed according to lipid bilayer studies a channel-forming activity of 0.6 nanosiemens in 1 m KCl. Single channel and selectivity measurements demonstrated that P13 had no preference for either cations or anions and showed no voltage-gating up to ±100 mV. Blue native polyacrylamide gel electrophoresis was used to isolate and characterize the P13 protein complex in its native state. The complex had a high molecular mass of about 300 kDa and was only composed of P13 monomers. The channel size was investigated using non-electrolytes revealing an apparent diameter of about 1.4 nm with a 400-Da mole

SUBMITTER: Barcena-Uribarri I 

PROVIDER: S-EPMC4081907 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature