Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product. 1999

G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
Department of Medicine, School of Medicine, University of North Carolina at Chapel Hill 27599, USA. gdbis@med.unc.edu

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.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D007781 Lactoferrin An iron-binding protein that was originally characterized as a milk protein. It is widely distributed in secretory fluids and is found in the neutrophilic granules of LEUKOCYTES. The N-terminal part of lactoferrin possesses a serine protease which functions to inactivate the TYPE III SECRETION SYSTEM used by bacteria to export virulence proteins for host cell invasion. Lactotransferrin
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009344 Neisseria gonorrhoeae A species of gram-negative, aerobic bacteria primarily found in purulent venereal discharges. It is the causative agent of GONORRHEA. Diplococcus gonorrhoeae,Gonococcus,Gonococcus neisseri,Merismopedia gonorrhoeae,Micrococcus der gonorrhoe,Micrococcus gonococcus,Micrococcus gonorrhoeae
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001425 Bacterial Outer Membrane Proteins Proteins isolated from the outer membrane of Gram-negative bacteria. OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial

Related Publications

G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
July 1984, The EMBO journal,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
January 1990, Proceedings of the National Academy of Sciences of the United States of America,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
June 1997, FEMS microbiology letters,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
February 1996, Molecular & general genetics : MGG,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
February 1998, Molecular microbiology,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
June 2018, Infection and immunity,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
November 1989, Infection and immunity,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
January 2014, Frontiers in microbiology,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
February 1984, The British journal of venereal diseases,
G D Biswas, and J E Anderson, and C J Chen, and C N Cornelissen, and P F Sparling
August 1996, Infection and immunity,
Copied contents to your clipboard!