BIOMAT Database Logo BIOMAT Database Logo

Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2. 1993

M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Transgène, Strasbourg, France.

Genes tbp1 and tbp2, encoding the transferrin-binding proteins Tbp1 and Tbp2, have been isolated from two strains of Neisseria meningitidis. The tbp2 and tbp1 open reading frames are tandemly arranged in the genome with an 87-bp intergenic region, and the DNA region upstream from the tbp2-coding sequence contains domains homologous to Escherichia coli promoter consensus motives. Nucleotide sequence analysis suggests the existence of a Tbp1 precursor carrying an N-terminal signal peptide with a peptidase I cleavage site and of a Tbp2 precursor with N-terminal homology to lipoproteins, including a peptidase II cleavage site. Comparison of the Tbp1 deduced amino acid (aa) sequences from both strains showed about 76% aa homology, while those of Tbp2 revealed only about 47% aa homology. These comparisons should be extended to other Neisseria strains in order to evaluate further this genetic divergence further.

UI MeSH Term Description Entries
D008074 Lipoproteins Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes. Circulating Lipoproteins,Lipoprotein,Lipoproteins, Circulating
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
D009345 Neisseria meningitidis A species of gram-negative, aerobic BACTERIA. It is a commensal and pathogen only of humans, and can be carried asymptomatically in the NASOPHARYNX. When found in cerebrospinal fluid it is the causative agent of cerebrospinal meningitis (MENINGITIS, MENINGOCOCCAL). It is also found in venereal discharges and blood. There are at least 13 serogroups based on antigenic differences in the capsular polysaccharides; the ones causing most meningitis infections being A, B, C, Y, and W-135. Each serogroup can be further classified by serotype, serosubtype, and immunotype. Diplokokkus intracellularis meningitidis,Meningococcus,Micrococcus intracellularis,Micrococcus meningitidis,Micrococcus meningitidis cerebrospinalis,Neisseria weichselbaumii
D011990 Receptors, Transferrin Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released. Transferrin Receptors,Transferrin Receptor,Receptor, Transferrin
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
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
D006090 Gram-Negative Bacteria Bacteria which lose crystal violet stain but are stained pink when treated by Gram's method. Gram Negative Bacteria
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
D000942 Antigens, Bacterial Substances elaborated by bacteria that have antigenic activity. Bacterial Antigen,Bacterial Antigens,Antigen, Bacterial

Related Publications

M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Diversity of the transferrin-binding protein Tbp2 of Neisseria meningitidis.
May 1995, Gene,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Molecular characterization of hybrid Tbp2 proteins from Neisseria meningitidis.
January 1996, Molecular microbiology,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin.
October 1994, Journal of bacteriology,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Cloning and sequencing of the gene encoding the outer-membrane protein Tbp1 from Actinobacillus pleuropneumoniae. Expression of Tbp1 and Tbp2.
February 1997, Behring Institute Mitteilungen,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Purification of the Neisseria meningitidis transferrin binding protein-2 (TBP2) to homogeneity using column chromatography.
May 1993, FEMS microbiology letters,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Cloning and characterization of the ponA gene encoding penicillin-binding protein 1 from Neisseria gonorrhoeae and Neisseria meningitidis.
April 1997, Journal of bacteriology,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Neisseria meningitidis expressing transferrin binding proteins of Actinobacillus pleuropneumoniae can utilize porcine transferrin for growth.
February 2000, Infection and immunity,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Blocking of iron uptake from transferrin by antibodies against the transferrin binding proteins in Neisseria meningitidis.
March 1996, Microbial pathogenesis,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Cloning and characterization of the Neisseria meningitidis rfaC gene encoding alpha-1,5 heptosyltransferase I.
June 1997, FEMS microbiology letters,
M Legrain, and V Mazarin, and S W Irwin, and B Bouchon, and M J Quentin-Millet, and E Jacobs, and A B Schryvers
Isolation and characterization of the haemin-binding proteins from Neisseria meningitidis.
June 1994, Microbiology (Reading, England),
Copied contents to your clipboard!