Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola.
A 53-kDa protein from the outer sheath of the oral spirochete Treponema denticola was purified to homogeneity and shown to reconstitute channels in black lipid bilayer model membranes. The channel had a single-channel conductance of 1.8 nS in 0.1 M KCl, making this the largest porin channel observed to date (estimated diameter, 3.4 nm). Electron micrographs of 53-kDa-protein-containing outer sheaths of T. denticola showed a regular hexagonal array of darker staining pits.
Egli
C
C
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Leung
W K
WK
Müller
K H
KH
Hancock
R E
RE
McBride
B C
BC
D000942:Antigens, Bacterial / Q000737:chemistry*; D000954:Antigens, Surface / Q000737:chemistry*; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004553:Electric Conductivity; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry*; D008567:Membranes, Artificial; D008854:Microscopy, Electron; D008970:Molecular Weight; D018272:Porins; D014208:Treponema / Q000737:chemistry* / Q000648:ultrastructure
D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008567:Membranes, Artificial; D018272:Porins