Binding characterization of the iron transport receptor from the outer membrane of Escherichia coli (FepA): differentiation between FepA and FecA.
The dissociation constants for the binding of ferric enterobactin with FepA and FecA are quantitated with displacement experiments. It is found that Kd for FepA is 12 times lower than the one for FecA. This indicates that FepA is an high-affinity receptor while FecA binds ferric enterobactin with a lower affinity. Monoclonal antibodies specific for binding epitopes of FepA inhibit the binding of ferric enterobactin with purified FepA. These same antibodies do not inhibit the binding of ferric enterobactin with purified FecA. This indicates that the binding epitopes in FecA and FepA are different.
Zhou
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XH
Department of Chemistry and Biochemistry, University of Oklahoma, Norman, USA.
van der Helm
D
D
Venkatramani
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L
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D004758:Enterobactin / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry*; D007501:Iron / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D011956:Receptors, Cell Surface; C029489:enterobactin receptor; D004758:Enterobactin; D007501:Iron