ArticleJournal of bacteriology2004
Transferrin-binding protein B of Neisseria meningitidis: sequence-based identification of the transferrin-Binding site confirmed by site-directed mutagenesis.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis of iron piracy by human gutProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-Wide Subtraction Analysis and Reverse Vaccinology to Detect Novel Drug Targets and Potential Vaccine Candidates Against Ehrlichia chaffeensis.Applied biochemistry and biotechnology · 2023Article
- Conformational instability of human prion protein upon residue modification: a molecular dynamics simulation study.EXCLI journal · 2014Article
- The transferrin-iron import system from pathogenic Neisseria species.Molecular microbiology · 2012Review
- Distribution of transferrin binding protein B gene (tbpB) variants among Neisseria species.BMC microbiology · 2008Article
- Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae.Infection and immunity · 2007Article
- Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A sequence-based prediction method was employed to identify three ligand-binding domains in transferrin-binding protein B (TbpB) of Neisseria meningitidis strain B16B6. Site-directed mutagenesis of residues located in these domains has led to the identification of two domains, amino acids 53 to 57 and 240 to 245, which are involved in binding to human transferrin (htf). These two domains are conserved in an alignment of different TbpB sequences from N. meningitidis and Neisseria gonorrhoeae, indicating a general functional role of the domains. Western blot analysis and BIAcore and isothermal titration calorimetry experiments demonstrated that site-directed mutations in both binding domains led to a decrease or abolition of htf binding. Analysis of mutated proteins by circular dichroism did not provide any evidence for structural alterations due to the amino acid replacements. The TbpB mutant R243N was devoid of any htf-binding activity, and antibodies elicited by the mutant showed strong bactericidal activity against the homologous strain, as well as against several heterologous tbpB isotype I strains.
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