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Pyoverdin‐facilitated iron uptake in Pseudomonas aeruginosa : immunological characterization of the ferripyoverdin receptor
Author(s) -
Meyer J. M.,
Hohnadel D.,
Khan A.,
Cornelis P.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00719.x
Subject(s) - siderophore , pseudomonas aeruginosa , antiserum , biology , polyclonal antibodies , bacterial outer membrane , receptor , blot , microbiology and biotechnology , pseudomonadaceae , pseudomonadales , immunofluorescence , membrane protein , membrane , biochemistry , bacteria , antibody , escherichia coli , gene , genetics , immunology
Summary A purified polyclonal antiserum directed against the isolated main 80kD IROMP (iron‐regulated outer‐membrane protein) from Pseudomonas aeruginosa PAO1 detected only the 80 kD polypeptide of outer‐membrane proteins from PAO1 cells grown in iron deficiency in Western blots. It was also shown to inhibit the uptake of 59 Fe pyoverdin by PAO1 cells as well as its binding to purified outer membranes. Immunofluorescence experiments with intact PAO1 cells confirmed that the receptor is present only at the surface of cells grown under conditions of iron deficiency. All these data allow us to conclude that the 80 kD main IROMP of P. aeruginosa is indeed the receptor for the siderophore ferripyoverdin.