Antibody inhibition of ferripyochelin binding to Pseudomonas aeruginosa cell envelopes

Abstract
A 14,000 MW (14K) protein which binds ferripyochelin was purified from cell envelopes of P. aeruginosa low Fe grown cells. The purified protein migrated as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and was shown to be free of contamination by lipopolysaccharide or carbohydrate. Rabbit antiserum to this protein reacted with the purified protein by immunoblot assay. The IgG fraction of this antiserum blocked binding of [59Fe]pyochelin to isolated cell envelopes of P. aeruginosa in a dose-dependent fashion.