Outer Membrane Proteins of Smooth and Rough Strains of Proteus mirabilis.

The outer membranes of the smooth Proteus mirabilis S1959 strain and its rough R13, R110, R51 and R45 mutants were isolated by sonication of the cells and sucrose density gradient centrifugation. The outer membrane of the rough strains had a lower density than that of their parent smooth strain, but the protein-to-phospholipid ratios were the same. The electrophoretic patterns of outer membrane polypeptides of the S and R strains in sodium dodecylsulfate/polyacrylamide gels were identical, with two major polypeptide bands, C1 and C2 (Mr 39000 and 38000) predominating. The C1 polypeptide band was a heat-modifiable polypeptide, which migrated as a band at Mr 33000 when membranes were solubilized at 37°C or 50°C, and at Mr 39000 when solubilization was at 100°C. Susceptibility of outer membrane polypeptides to proteolytic digestion was found to be higher in isolated outer membrane preparations of the rough strains than in the smooth strain, suggesting that the availability of the polypeptide chains to proteolytic activity depends on the length of the polysaccharide chains of the outer membrane lipopolysaccharide. [ABSTRACT FROM AUTHOR]

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