DOI: 10.1128/IAI.67.1.455-459.1999
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.
- Copyright © 1999 American Society for Microbiology