Bacteriostatic enterochelin-specific immunoglobulin from normal human serum.

Heat-inactivated normal human serum produces iron-reversible bacteriostasis of a number of microorganisms. This inhibitory effect was abolished by adsorption of serum with ultraviolet-killed cells of species that produce the siderophore enterochelin. Bacteriostasis also was alleviated by adsorption of serum with 2,3-dihydroxy-N-benzoyl-L-serine, a degradation product of enterochelin, bound to the insoluble matrix AH-Sepharose 4B. The adsorption process did not add iron or enterochelin to serum, nor did it remove transferrin. The immunoglobulin fraction from normal human serum was isolated; when added to a defined medium (M199) prepared so as to mimic normal human serum, the immunoglobulin rendered the medium inhibitory to an enterochelin-defective strain of Salmonella typhimurium. Adsorption of this medium with AH-Sepharose 4B-2,3-dihydroxy-N-benzoyl-L-serine removed the inhibition. Our results indicate that enterochelin-specific immunoglobulins exist in normal human serum. These immunoglobulins may act synergistically with transferrin to effect bacteriostasis of enterochelin-producing pathogens.