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Infection and Immunity, January 1999, p. 455-459, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification and Functional Characterization of the Neisseria gonorrhoeae lbpB Gene Product

Gour D. Biswas,1,* James E. Anderson,1 Ching-Ju Chen,1 Cynthia Nau Cornelissen,2 and P. Frederick Sparling1,3

Department of Medicine1 and Department of Microbiology and Immunology,3 School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, and Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, Virginia 232982

Received 10 July 1998/Returned for modification 18 August 1998/Accepted 20 October 1998

We cloned lbpB, encoding a predicted 80-kDa lipoprotein, upstream of lbpA. A nonpolar mutant (LbpB- LbpA+) had normal lactoferrin (LF) binding and grew normally with LF as an iron source, whereas LbpB- LbpA- and LbpB+ LbpA- strains had reduced binding of LF and did not grow with LF as an iron source. LbpB bound LF directly in an affinity purification, suggesting that LbpB might play a still-uncharacterized role in the LF iron utilization.

* Corresponding author. Mailing address: Department of Medicine, University of North Carolina at Chapel Hill, CB# 7030, Chapel Hill, NC 27599-7005. Phone: (919) 966-3661. Fax: (919) 966-6714. E-mail: gdbis{at}med.unc.edu.

Infection and Immunity, January 1999, p. 455-459, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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Copyright © 1999 by the American Society for Microbiology. All rights reserved.