Binding characterization of the iron transport receptor from the outer membrane of Escherichia coli (FepA): differentiation between FepA and FecA

X H Zhou; D van der Helm; L Venkatramani

doi:10.1007/BF00142012

Binding characterization of the iron transport receptor from the outer membrane of Escherichia coli (FepA): differentiation between FepA and FecA

Biometals. 1995 Apr;8(2):129-36. doi: 10.1007/BF00142012.

Authors

X H Zhou¹, D van der Helm, L Venkatramani

Affiliation

¹ Department of Chemistry and Biochemistry, University of Oklahoma, Norman, USA.

PMID: 7734925
DOI: 10.1007/BF00142012

Abstract

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.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Bacterial Outer Membrane Proteins / metabolism*
Carrier Proteins / metabolism*
Enterobactin / metabolism
Escherichia coli / chemistry*
Iron / metabolism*
Receptors, Cell Surface / metabolism*

Substances

Bacterial Outer Membrane Proteins
Carrier Proteins
Receptors, Cell Surface
enterobactin receptor
Enterobactin
Iron

Grants and funding

GM21822/GM/NIGMS NIH HHS/United States