Bordetella pertussis major outer membrane porin protein forms small, anion-selective channels in lipid bilayer membranes.

Abstract:

:The major outer membrane protein of molecular weight 40,000 (the 40K protein) of a virulent isolate of Bordetella pertussis was purified to apparent homogeneity. The purified protein formed an oligomer band (of apparent molecular weight 90,000) on sodium dodecyl sulfate-polyacrylamide gels after solubilization at low temperatures. The porin function of this protein was characterized by the black lipid bilayer method. The 40K protein formed channels smaller than all other constitutive major outer membrane porins studied to date. The average single-channel conductance in 1 M KCl was 0.56 nS. This was less than a third of the conductance previously observed for Escherichia coli porins. Zero-current potential measurements made of the porin to determine its ion selectivity revealed the porin to be more than 100-fold selective for anions over cations. The single-channel conductance was measured as a function of salt concentration. The data could be fitted to a Lineweaver-Burk plot suggesting an anion binding site with a Kd of 1.17 M Cl- and a maximum possible conductance through the channel of 1.28 nS.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Armstrong SK,Parr TR Jr,Parker CD,Hancock RE

doi

10.1128/jb.166.1.212-216.1986

subject

Has Abstract

pub_date

1986-04-01 00:00:00

pages

212-6

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

166

pub_type

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