Gd. Biswas et al., Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product, INFEC IMMUN, 67(1), 1999, pp. 455-459
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, suggestin
g that LbpB might play a still-uncharacterized role in the LF iron utilizat
ion.