OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity.

Journal article

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.

Authors: Law, C; Penfold, C; Walker, D; Moore, G; James, R

• Journal: FEBS letters
• Volume: 545
• Issue: 2-3
• Pages: 127-132
• Publication date: 2003-06-01
• DOI: 10.1016/s0014-5793(03)00511-8
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Escherichia coli Proteins; Protein Structure, Secondary; Colicins; Escherichia coli; Spectrophotometry, Ultraviolet; Receptors, Peptide; Circular Dichroism; Membrane Transport Proteins; Protein Structure, Tertiary; Bacterial Outer Membrane Proteins; Vitamin B 12; Protein Binding; Cross-Linking Reagents