Paulin, S; Jamshad, M; Dafforn, TR; Garcia-Lara, J; Foster, SJ; Galley, NF; Roper, DI; ... Taylor, PW; + view all Paulin, S; Jamshad, M; Dafforn, TR; Garcia-Lara, J; Foster, SJ; Galley, NF; Roper, DI; Rosado, H; Taylor, PW; - view fewer (2014) Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. Nanotechnology , 25 (28) 285101 - ?. 10.1088/0957-4484/25/28/285101.

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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.

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