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OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity
Author(s) -
Law Christopher J,
Penfold Christopher N,
Walker Daniel C,
Moore Geoffrey R,
James Richard,
Kleanthous Colin
Publication year - 2003
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(03)00511-8
Subject(s) - colicin , bacterial outer membrane , escherichia coli , biology , porin , microbiology and biotechnology , biochemistry , gene
The outer membrane (OM) vitamin B 12 receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli . Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9–BtuB complexes could be readily shown in vitro, OmpF‐containing complexes could not be detected, implying that OmpF association with the BtuB–colicin complex, while necessary, must be weak and/or transient in nature.