Reconstitution of Model Membranes from Phospholipid and Outer Membrane Proteins of Proteus mirabilis

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Abstract
Outer membrane proteins extracted from isolated cell walls of P. mirabilis combined with cell wall phospholipids in a model membrane system. The presence of outer membrane proteins in vesicular model membranes mediated the release of previously entrapped [14C]sucrose while [3H]inulin was retained. Incorporation of lipopolysaccharide from the same cell walls was not required for the formation of such selectively permeable membranes. Three major outer membrane proteins of apparent MW 39,000, 36,000 and 17,000 were isolated using acetic acid and sodium deoxycholate solution as solvents and avoiding the strongly denaturing sodium dodecyl sulfate. The isolated proteins were assayed for their ability to form hydrophilic pores in reconstituted membranes. The trypsin-sensitive 39,000 MW protein and the peptidoglycan-associated 36,000 MW protein were equally effective in this function but the 17,000 MW protein mediated little penetration of low MW solute. The 39,000 MW and 36,000 MW proteins also protected reconstituted membrane vesicles from disruption by detergent while 17,000 MW protein was ineffective in this regard.

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