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

Research output: Contribution to journalArticle


  • Sarah Paulin
  • Jorge Garcia-lara
  • Simon J Foster
  • Nicola F Galley
  • David I Roper
  • Helena Rosado
  • Peter W Taylor

Colleges, School and Institutes


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 languageEnglish
Article number285101
Issue number28
Publication statusPublished - 18 Jul 2014


  • Staphylococcus aureus, poly(styrene-co-maleic acid), lipid nanoparticles, antibiotic resistance, immunoaffinity chromatography