Understanding the insertion of antibiotic toxins into the gram negative outer bacterial membrane

DOI

The gram-negative bacterial membrane is of extreme medical importance. Two of its major components are lipopolysaccharides (LPS's) and integral membrane proteins. Porins are beta-barrel, pore-forming, membrane proteins found in the outer membrane of gram-negative bacteria. We have produced and examined Porin-lipid monolayers at the air/liquid interface and used this to examine bacterial toxin-membrane interactions. The porin OmpF is the receptor for the antibacterial toxin colicin N and enables the toxin to translocate across the bacterial outer membrane in order to kill E coli cells. Here, we propose to examine the interaction of engineered colicins with OmpF-LipidA (the membrane bound portion of LPS) monolayers. Aiming to determine the mechanism of Colicin-bacterial membrane interactions as well as similarities and differences between the activities of differing colicin types.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24086392
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24086392
Provenance
Creator Dr Luke Clifton; Professor Jeremy Lakey; Dr Chris Johnson; Dr Stephen Holt; Ms Nat Arunmanee
Publisher ISIS Neutron and Muon Source
Publication Year 2014
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2011-07-17T06:50:53Z
Temporal Coverage End 2011-07-22T03:50:55Z