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High‐conductance channel induced by the interaction of phage lambda with its receptor maltoporin
Author(s) -
Berrier Catherine,
Bonhivers Melanie,
Letellier Lucienne,
Ghazi Alexandre
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01705-1
Subject(s) - lambda phage , liposome , biophysics , conductance , lipid bilayer , bacteriophage , lambda , chemistry , membrane , bilayer , biology , biochemistry , escherichia coli , physics , gene , condensed matter physics , optics
Bacteriophage λ that binds to liposomes bears its receptor maltoporin (LamB) and is able to inject its DNA into the internal space. During this process, the liposomes are permeabilized, suggesting that a transmembrane channel has formed (Roessner and Ihler (1986) J. Biol. Chem. 261, 386–390). This pore possibly constitutes the pathway used by λ DNA to cross the membrane. We reconstituted purified LamB from Shigella in liposomes that were incubated with λ phages. Addition of this mixture to a bilayer chamber resulted in the incorporation in planar bilayers of high‐conductance channels whose conductance, kinetics and voltage dependence were totally different from those of maltoporin channels.