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.
Original language | English |
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Article number | 285101 |
Journal | Nanotechnology |
Volume | 25 |
Issue number | 28 |
DOIs | |
Publication status | Published - 18 Jul 2014 |
Keywords
- Staphylococcus aureus
- poly(styrene-co-maleic acid)
- lipid nanoparticles
- antibiotic resistance
- immunoaffinity chromatography