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Bacterial transferrin and lactoferrin receptors.
Pathogenic members of the Neisseriaceae and Pasteurellaceae express outer-membrane receptor proteins involved in the direct assimilation of iron from the host glycoproteins transferrin andExpand
Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis
Isogenic mutants constructed in the tbpA and tbpB genes from Neisseria meningitidis strain B16B6 demonstrated a reduced transferrin binding activity in intact cells and total membranes but were incapable of utilizing transferrin iron for growth. Expand
Identification and characterization of the transferrin receptor from Neisseria meningitidis
Growth studies with iron‐deficient cells and competition binding experiments demonstrated that the meningococcal receptor was species‐specific for human transferrin. Expand
Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2.
Comparisons should be extended to other Neisseria strains in order to evaluate further this genetic divergence further, and the existence of a Tbp1 precursor carrying an N-terminal signal peptide with a peptidase I cleavage site and a TBP2 precursor with N- terminal homology to lipoproteins is suggested. Expand
Culture and molecular-based profiles show shifts in bacterial communities of the upper respiratory tract that occur with age
The resulting profiles suggest that in young children the nasopharyngeal microbiota, much like the gastrointestinal tract microbiome, changes from an immature state, where it is colonized by a few dominant taxa, to a more diverse state as it matures to resemble the adult microbiota. Expand
Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
Competition binding assays demonstrated that the binding of lact oferrin was specific for human lactoferrin in that neither bovine lactoferin, human transferrin, nor human hemoglobin was able to block binding of HRP-lactoferrIn. Expand
Iron acquisition systems in the pathogenic Neisseria
Preliminary pilot studies indicate that transferrin receptor‐based vaccines may be protective in humans, and the receptors are potentially ideal vaccine targets in view of their critical role in survival in the host. Expand
The Transferrin Binding Protein B of Moraxella catarrhalis Elicits Bactericidal Antibodies and Is a Potential Vaccine Antigen
The deduced sequences of the M. catarrhalis TbpA proteins from two strains were 98% identical, while those of the TbpB proteins from the same strains were 63% identical and 70% similar, and if bactericidal ability is clinically relevant, a vaccine comprising multiple rTbpB antigens may protect against M. catcherhalis disease. Expand
Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida
Results suggest that P. multocida has a single, novel receptor protein (TbpA) that is capable of efficiently mediating iron acquisition from bovine transferrin without the involvement of a second receptor protein(TbpB). Expand
Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae.
The transferrin receptor was specific for human transferrin and the lactoferrin receptor had a high degree of specificity for human lact oferrin in all species tested. Expand