Specific inhibition of Escherichia coli ferrienterochelin uptake by a normal human serum immunoglobulin.

Normal human serum contains an enterochelin-specific antibody which presumably acts with transferrin to hinder iron assimilation by enterochelin-producing pathogens. This antibody can be isolated from serum by sodium sulfate fractionation or affinity chromatography by employing an enterochelin-derived ligand (2,3-dihydroxy-N-benzoyl-L-serine) attached to aminohexyl Sepharose 4B. In assays of iron uptake by whole cells, the antibody inhibited enterochelin-directed uptake but not that mediated by citrate or ferrichrome. Also, the growth stimulatory effect of enterochelin on an Ent- strain of Escherichia coli was blocked by the immunoglobulin. This antibody has a high affinity for enterochelin; various elution procedures employing high salt concentrations and low pH failed to remove it from affinity columns. Elution with 3 M sodium thiocyanate or 13 mM 2,3-dihydroxybenzoic acid proved successful. Two pieces of evidence indicate the enterochelin-specific antibody is primarily of the immunoglobulin A (IgA) isotype. It could be removed from serum with goat antihuman IgA and was present only in sodium sulfate fractions of serum known to contain IgA.