ArticlePLoS pathogens2017
Lactoferrin binding protein B - a bi-functional bacterial receptor protein.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Review
- The Association Between Maternal Diet and the Human Milk Microbiome: A Review of Evidence and Methodological Challenges.Microorganisms · 2025Review
- Bacterial hemophilin homologs and their specific type eleven secretor proteins have conserved roles in heme capture and are diversifying as a family.Journal of bacteriology · 2024Article
- Targeting Intracellular Bacteria with Dual Drug-loaded Lactoferrin Nanoparticles.ACS infectious diseases · 2024Article
- A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase-separated droplets.PNAS nexus · 2024Article
- Testing Antimicrobial Properties of Human Lactoferrin-Derived Fragments.International journal of molecular sciences · 2023Article
- Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.Pharmaceutics · 2023Review
- Lactoferrin-based food supplements trigger toxin production of enteropathogenicFrontiers in microbiology · 2023Article
- Correlation ofEmerging microbes & infections · 2022Article
- Lactoferrin Alleviates Lipopolysaccharide-Induced Infantile Intestinal Immune Barrier Damage by Regulating an ELAVL1-Related Signaling Pathway.International journal of molecular sciences · 2022Article
- Nutritional immunity: the battle for nutrient metals at the host-pathogen interface.Nature reviews. Microbiology · 2022Review
- Antimicrobial activity of bovine lactoferrin againstFrontiers in microbiology · 2022Article
- Article
- The Role of theFrontiers in microbiology · 2021Article
- Lactoferrin in Human Milk of Prolonged Lactation.Nutrients · 2019Article
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.The Journal of biological chemistryReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Lactoferrin binding protein B (LbpB) is a bi-lobed outer membrane-bound lipoprotein that comprises part of the lactoferrin (Lf) receptor complex in Neisseria meningitidis and other Gram-negative pathogens. Recent studies have demonstrated that LbpB plays a role in protecting the bacteria from cationic antimicrobial peptides due to large regions rich in anionic residues in the C-terminal lobe. Relative to its homolog, transferrin-binding protein B (TbpB), there currently is little evidence for its role in iron acquisition and relatively little structural and biophysical information on its interaction with Lf. In this study, a combination of crosslinking and deuterium exchange coupled to mass spectrometry, information-driven computational docking, bio-layer interferometry, and site-directed mutagenesis was used to probe LbpB:hLf complexes. The formation of a 1:1 complex of iron-loaded Lf and LbpB involves an interaction between the Lf C-lobe and LbpB N-lobe, comparable to TbpB, consistent with a potential role in iron acquisition. The Lf N-lobe is also capable of binding to negatively charged regions of the LbpB C-lobe and possibly other sites such that a variety of higher order complexes are formed. Our results are consistent with LbpB serving dual roles focused primarily on iron acquisition when exposed to limited levels of iron-loaded Lf on the mucosal surface and effectively binding apo Lf when exposed to high levels at sites of inflammation.
Indexed as
Identifiers
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.