Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product.
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.
Biswas
G D
GD
Department of Medicine, School of Medicine, University of North Carolina at Chapel Hill 27599, USA. gdbis@med.unc.edu
Anderson
J E
JE
Chen
C J
CJ
Cornelissen
C N
CN
Sparling
P F
PF
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D005798:Genes, Bacterial / Q000502:physiology*; D007501:Iron / Q000378:metabolism; D007781:Lactoferrin / Q000378:metabolism*; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000235:genetics* / Q000502:physiology; D011956:Receptors, Cell Surface / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; C112566:LBPA protein, Neisseria meningitidis; D011956:Receptors, Cell Surface; D007501:Iron; D007781:Lactoferrin