Purification and characterization of a major 40 kDa outer membrane protein of Acinetobacter baumannii

AbstractAcinetobacter baumannii, an opportunistic pathogen, is well known to cause a wide spectrum of nosocomial infections particularly in intensive care units. The major outer membrane (OM) protein, OmpAb, of 40 kDa from A. baumannii has been identified and purified to homogeneity from cultures grown at 30°C and 100 mM NaCl. The synthesis of OM proteins of A. baumannii is thermoregulated and osmoregulated. The pore forming ability of the purified OmpAb and the diffusion of uncharged solutes in proteoliposomes has been demonstrated by following the liposomal swelling assay. The trimeric OmpAb is characterized as a porin with a pore size of 1.3 nm and is found to be similar to the OmpF of Escherichia coli and can possibly be classified as a general diffusion pore. It appears that OmpAb plays an important role in the diffusion properties of the outer membrane of A. baumannii