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Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product.

ABSTRACT: 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.

SUBMITTER: Biswas GD 

PROVIDER: S-EPMC96337 | biostudies-literature | 1999 Jan

REPOSITORIES: biostudies-literature

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Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product.

Biswas G D GD   Anderson J E JE   Chen C J CJ   Cornelissen C N CN   Sparling P F PF  

Infection and immunity 19990101 1

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. ...[more]

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