Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes ofEscherichia coliUT5600/pBB2

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...

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...

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...

The Journal of General Physiology Concerted loop motion triggers induced fit of FepA to ferric enterobactin

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...