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Journal of Bacteriology, May 1999, p. 2895-2901, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Ferric Enterobactin Binding and Utilization by Neisseria gonorrhoeae

Susan D. Biegel Carson,1 Philip E. Klebba,2 Salete M. C. Newton,2 and P. Frederick Sparling1,3,*

Department of Microbiology and Immunology1 and Department of Medicine,3 University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, and Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 730192

Received 23 December 1998/Accepted 19 February 1999

FetA, formerly designated FrpB, an iron-regulated, 76-kDa neisserial outer membrane protein, shows sequence homology to the TonB-dependent family of receptors that transport iron into gram-negative bacteria. Although FetA is commonly expressed by most neisserial strains and is a potential vaccine candidate for both Neisseria gonorrhoeae and Neisseria meningitidis, its function in cell physiology was previously undefined. We now report that FetA functions as an enterobactin receptor. N. gonorrhoeae FA1090 utilized ferric enterobactin as the sole iron source when supplied with ferric enterobactin at approximately 10 µM, but growth stimulation was abolished when an omega (Omega ) cassette was inserted within fetA or when tonB was insertionally interrupted. FA1090 FetA specifically bound 59Fe-enterobactin, with a Kd of approximately 5 µM. Monoclonal antibodies raised against the Escherichia coli enterobactin receptor, FepA, recognized FetA in Western blots, and amino acid sequence comparisons revealed that residues previously implicated in ferric enterobactin binding by FepA were partially conserved in FetA. An open reading frame downstream of fetA, designated fetB, predicted a protein with sequence similarity to the family of periplasmic binding proteins necessary for transporting siderophores through the periplasmic space of gram-negative bacteria. An Omega  insertion within fetB abolished ferric enterobactin utilization without causing a loss of ferric enterobactin binding. These data show that FetA is a functional homolog of FepA that binds ferric enterobactin and may be part of a system responsible for transporting the siderophore into the cell.

* Corresponding author. Mailing address: Department of Medicine, University of North Carolina at Chapel Hill, C. B. 7030, Chapel Hill, NC 27599. Phone: (919) 966-3661. Fax: (919) 966-6714. E-mail: zman{at}med.unc.edu.

Journal of Bacteriology, May 1999, p. 2895-2901, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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