passive immunization by recombinant ferric enterobactin protein (fepa) from escherichia coli o157.

Passive immunization by recombinant ferric enterobactin protein (FepA) from Escherichia coli O157

BACKGROUND AND OBJECTIVES Enterohemorrhagic Escherichia coli (EHEC) O157:H7 has been recognized as a major food borne pathogen responsible for frequent hemorrhagic colitis and hemolytic uremic syndrome in humans. Cattle are important reservoirs of E. coli O157:H7, in which the organism colonizes the intestinal tract and is shed in the feces. OBJECTIVE Vaccination of cattle has significant pot...

antibody production against enterobacteriacea using recombinant ferric enterobactin protein (fepa)

objective: escherichia coli o157:h7 is a gram-negative rod-shaped bacterium. e coli o157:h7 is an enterohemorrhagic (ehec) strain of the bacterium escherichia coli and a cause of foodborne illness. infection often leads to bloody diarrhea by producing a toxin called shiga toxin, which damages the intestines, and occasionally leads to kidney failure, especially in young children and elderly peop...

Aromatic components of two ferric enterobactin binding sites in Escherichia coli FepA.

Ferric enterobactin is a catecholate siderophore that binds with high affinity (Kd approximately 10-10 M) to the Escherichia coli outer membrane protein FepA. We studied the involvement of aromatic amino acids in its uptake by determining the binding affinities, kinetics and transport properties of site-directed mutants. We replaced seven aromatic residues (Y260, Y272, Y285, Y289, W297, Y309 an...

Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB.

The periplasmic protein FepB of Escherichia coli is a component of the ferric enterobactin transport system. We overexpressed and purified the binding protein 23-fold from periplasmic extracts by ammonium sulfate precipitation and chromatographic methods, with a yield of 20%, to a final specific activity of 15,500 pmol of ferric enterobactin bound/mg. Periplasmic fluid from cells overexpressing...

Recognition and transport of ferric enterobactin in Escherichia coli.

The specificity of the outer membrane protein receptor for ferric enterobactin transport in Escherichia coli and the mechanism of enterobactin-mediated transport of ferric ions across the outer membrane have been studied. Transport kinetic and inhibition studies with ferric enterobactin and synthetic structural analogs have mapped the parts of the molecule important for receptor binding. The fe...

Advances and challenges in recombinant protein expression in Escherichia coli