Format

Send to

Choose Destination
Nanotechnology. 2014 Jul 18;25(28):285101. doi: 10.1088/0957-4484/25/28/285101. Epub 2014 Jun 27.

Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a.

Author information

1
School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UK.

Abstract

Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of the cell division machinery from the membrane of drug-resistant staphylococcal cells. SMA-lipid nanoparticles solubilized FtsZ-PBP2-PBP2a complexes from intact cells, demonstrating the close physical proximity of these proteins within the lipid bilayer. Exposure of bacteria to (-)-epicatechin gallate, a polyphenolic agent that abolishes β-lactam resistance in staphylococci, disrupted the association between PBP2 and PBP2a. Thus, SMA purification provides a means to remove native integral membrane protein assemblages with minimal physical disruption and shows promise as a tool for the interrogation of molecular aspects of bacterial membrane protein structure and function.

PMID:
24972373
DOI:
10.1088/0957-4484/25/28/285101
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for IOP Publishing Ltd.
Loading ...
Support Center