Lipoprotein from the outer membrane of Escherichia coli: purification, paracrystallization, and some properties of its free form.

SDS-PAGE Analysis of the Outer Membrane Proteins of Uropathogenic Escherichia coli Isolated from Patients in Different Wards of Nemazee Hospital, Shiraz, Iran

Background: Outer membrane proteins (OMPs) constitute the main structure and about half of the cell wall of Gram-negative bacteria. The OMPs of Escherichia coli (E. coli) play an important role in its drug resistance. Previous studies have shown that the OMPs of E. coli enhance its pathogenic effects by helping the bacterium to evade the immune defense and promote its adsorption to host cells. ...

Immunogenicity of enterotoxigenic Escherichia coli outer membrane vesicles encapsulated in chitosan nanoparticles

Objective(s): Enterotoxigenic Escherichia coli (ETEC) is an important cause of diarrheal disease in humans, particularly in children under 5 years and travelers in developing countries. To our knowledge, no vaccine is licensed yet to protect against ETEC infection. Like many Gram-negative pathogens, ETEC can secrete outer membrane vesicles (OMVs). These structures contain various immunogenic vi...

A Chimeric Vaccine Consisting of Highly Immunogenic Regions form Escherichia coli Iron Regulated Outer-Membrane Proteins: An In Silico Approach

Apolipoprotein, an intermediate in the processing of the major lipoprotein of the Escherichia coli outer membrane.

A new intermediate (apolipoprotein) in the synthesis of the major lipoprotein of the Escherichia coli outer membrane has been identified. The accumulation of this new form of the lipoprotein was observed when excessive production of lipoprotein was induced or when the membrane fraction containing the prolipoprotein accumulated in the presence of globomycin was incubated at 60 degrees C. The new...

Spin labeling of a cysteine residue of the Escherichia coli outer membrane lipoprotein in its membrane environment.

A method was developed to attach a spin label to a specific site on the structural lipoprotein of the Escherichia coli outer membrane in situ. This method takes advantage of the fact that the outer membrane of wild-type E. coli contains few residues reactive towards sulfhydryl reagents. A mutant E. coli strain has been isolated [Suzuki, H., Nishimura, Y., Iketani, H., Campisi, J., Hirashima, A....