ArticleThe Journal of biological chemistry2011
Anchor peptide of transferrin-binding protein B is required for interaction with transferrin-binding protein A.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Temporal Dynamics of T Cell Immunity Induced by TbpBVeterinary sciences · 2026Article
- TbpB-based oral mucosal vaccine provides heterologous protection against Glässer's disease caused by different serovars of Spanish field isolates of Glaesserella parasuis.Porcine health management · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Targeting bacterial transferrin and lactoferrin receptors for vaccines.Trends in microbiology · 2022Review
- Insights from targeting transferrin receptors to develop vaccines for pathogens of humans and food production animals.Frontiers in cellular and infection microbiology · 2022Article
- Development of a non-biased, high-throughput ELISA for the rapid evaluation of immunogenicity and cross-reactivity.Journal of immunological methods · 2021Article
- The Role of theFrontiers in microbiology · 2021Article
- Utility of Hybrid Transferrin Binding Protein Antigens for Protection Against Pathogenic Neisseria Species.Frontiers in immunology · 2019Article
- Lactoferrin binding protein B - a bi-functional bacterial receptor protein.PLoS pathogens · 2017Article
- Patterns of structural and sequence variation within isotype lineages of the Neisseria meningitidis transferrin receptor system.MicrobiologyOpen · 2015Article
- Nonbinding site-directed mutants of transferrin binding protein B exhibit enhanced immunogenicity and protective capabilities.Infection and immunity · 2015Article
- The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides.PloS one · 2014Article
- Conserved regions of gonococcal TbpB are critical for surface exposure and transferrin iron utilization.Infection and immunity · 2013Article
- Characterization of a ferrous iron-responsive two-component system in nontypeable Haemophilus influenzae.Journal of bacteriology · 2012Article
- The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-negative bacterial pathogens belonging to the Pasteurellaceae, Moraxellaceae, and Neisseriaceae families rely on an iron acquisition system that acquires iron directly from host transferrin (Tf). The process is mediated by a surface receptor composed of transferrin-binding proteins A and B (TbpA and TbpB). TbpA is an integral outer membrane protein that functions as a gated channel for the passage of iron into the periplasm. TbpB is a surface-exposed lipoprotein that facilitates the iron uptake process. In this study, we demonstrate that the region encompassing amino acids 7-40 of Actinobacillus pleuropneumoniae TbpB is required for forming a complex with TbpA and that the formation of the complex requires the presence of porcine Tf. These results are consistent with a model in which TbpB is responsible for the initial capture of iron-loaded Tf and subsequently interacts with TbpA through the anchor peptide. We propose that TonB binding to TbpA initiates the formation of the TbpB-TbpA complex and transfer of Tf to TbpA.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.