Pinning down pinholin: a structural mechanism to explain how peptide adsorption at bacterial membranes controls viral infections

DOI

We will use specular and off-specular neutron reflectivity to provide a structural mechanism for the way in which the amphipathic peptide pinholin controls bacterial cell lysis and hence infection of bacteria by phage lambda. In vivo studies have suggested a mechanism whereby pinholin is initially uniformly distributed across the inner leaflet of the inner bacterial membrane until a critical coverage is reached at which point they redistribute into 100 nm diameter rafts and then collectively rearrange into a series of 2 nm channel diameter heptameric transmebrane pores. Contrast variation and specular reflectivity from floating bilayer will allow peptide pores (high solvent penetration) to be distinguished from uniform peptide distribution. Off-specular measurements will allow this transition to be correlated to raft size. The combination will enable the pore size to be measured.

Identifier
DOI https://doi.org/10.5286/ISIS.E.49917947
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/49917947
Provenance
Creator Miss Laura McKinley; Dr Rob Barker; Dr Simon Titmuss; Dr Stephen Roser
Publisher ISIS Neutron and Muon Source
Publication Year 2017
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 Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2014-05-30T23:00:00Z
Temporal Coverage End 2014-06-04T09:00:52Z