| Bacterial outer membrane proteins are suitable targets for the antimicrobial drugs and vaccine development. Our work focused on three outer membrane proteins: OmpT of Escherichia coli, Tsh of avian pathogenic E. coli, and Omp85 of Yersinia pestis.; We showed that the purified OmpT protease could adhere to laminin and fibronectin. Our evolutionary analysis identified new of omptin proteins.; Tsh is a conventional autotransporter and a virulence factor. Our in vitro quaternary structure study employed a cross-linking and a blue-native PAGE and demonstrated that the purified Tsh formed monomers or dimers.; We presented a quaternary structure study of Omp85 a conserved protein important for bacterial survival and biogenesis of outer membrane proteins. Y. pestis omp85 gene was cloned and expressed. Omp85 was shown to form monomers, dimers, and tetramers in vitro using cross-linking, semi-native PAGE, and sedimentation studies. In vivo studies indicated that Omp85 formed tetramers. Our studies contributed to a better understanding of Omp85 structure and mechanism.; Our research provided a functional and structural characterization of three classes of bacterial outer membrane proteins. The applied relevance of this work has potential use in the development of new vaccines and antimicrobials, which may be potent weapons in a fight against bacterial infections. |
