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Appl. Environ. Microbiol., Feb 1997, 524-531, Vol 63, No. 2
Copyright © 1997, American Society for Microbiology

Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure

Y Chen, R Shapira, M Eisenstein and TJ Montville
Department of Food Science, New Jersey Agricultural Experiment Station, Cook College, Rutgers, State University of New Jersey, New Brunswick 08903-0231, USA.

The physicochemical interaction of pediocin PA-1 with target membranes was characterized using lipid vesicles made from the total lipids extracted from Listeria monocytogenes. Pediocin PA-1 caused the time- and concentration-dependent release of entrapped carboxyfluorescein (CF) from the vesicles. The pediocin-induced CF efflux rates were higher under acidic conditions than under neutral and alkaline conditions and were dependent on both pediocin and lipid concentrations. A binding isotherm constructed on the basis of the Langmuir isotherm gave an apparent binding constant of 1.4 x 10(7) M-1 at pH 6.0. The imposition of a transmembrane potential (inside negative) increased the CF efflux rate by 88%. Pediocin PA-1 also permeablized synthetic vesicles composed only of phosphatidylcholine. Sequence alignments and secondary-structure predictions for the N terminus of pediocin PA-1 and other class IIa bacteriocins predicted that pediocin PA-1 contained two beta-sheets maintained in a hairpin conformation stabilized by a disulfide bridge. The structural model also revealed patches of positively charged residues, consistent with the argument that electrostatic interactions play an important role in the binding of pediocin PA-1 to the lipid vesicles. This study demonstrates that pediocin PA-1 can function in the absence of a protein receptor and provides a structural model consistent with these results.


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