The gene encoding porin protein F of Pseudomonas aeruginosa was cloned onto a cosmid vector into Escherichia coli. Protein F was expressed as the predominant outer membrane protein in a porin-deficient E. coli background and was clearly visible on one-dimensional sodium dodecyl sulfate-polyacrylamide gels in a porin-sufficient background. The identity of the protein F from the E. coli clone and...

Pseudomonas aeruginosa OprF is a largely monomeric outer membrane protein that allows the slow, nonspecific transmembrane diffusion of solutes. This protein folds into two different conformers, with the majority conformer folding into a two-domain conformation that has no porin activity and the minority conformer into a one-domain conformation with high porin activity and presumably consisting ...

Mouse monoclonal antibodies were raised against recombinant Salmonella typhi 36-kDa porin monomer. Specificities of 16 monoclonal antibodies were analyzed as reactivity patterns in dot immunobinding and Western blot (immunoblot) assays using isolated outer membrane proteins of gram-negative bacteria and cloned purified S. typhi porin monomers and trimers. Four monoclonal antibodies were specifi...

Objective(s): The porins A and B and also outer membrane vesicles (OMVs) of Neisseria meningitidis are used for vaccine purposes. In the present study, we aimed to design a new vaccine candidate based on a fusion of PorA of serogroups A and B of N. meningitidis admixed with OMV and evaluate it in an animal model.Materials and Methods: Af...

background and objectives: the oprd mutation and ampc overproduction are the main mechanisms of intrinsic resistance to carbapenems such as imipenem and meropenem in pseudomonas aeruginosa . materials and methods: in this study, we investigated intrinsic resistance to carbapenems including mutation of oprd and ampc overproduction in a carbapenem-resistant p. aeruginosa isolated from a burn pati...

Pseudomonas aeruginosa OprF forms 0.36-nS channels and, rarely, 2- to 5-nS channels in lipid bilayer membranes. We show that a protein comprising only the N-terminal 162-amino-acid domain of OprF formed the smaller, but not the larger, channels in lipid bilayers. Circular dichroism spectroscopy indicated that this protein folds into a beta-sheet-rich structure, and three-dimensional comparative...

Two major outer membrane proteins of Enterobacter cloacae 206 were purified and identified as porins by using reconstituted vesicles. The 37-kilodalton porin forms a channel with a radius of 0.6 nm, which prefers positively charged substances to negatively charged ones, whereas the 39- to 40-kilodalton porin forms a larger channel with a radius of 0.8 nm, which has weaker selectivity for electr...