ArticleProceedings of the National Academy of Sciences of the United States of America1997
An opsonic function of the neutrophil bactericidal/permeability-increasing protein depends on both its N- and C-terminal domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 159 citations in OpenAlex.
- Expression of bactericidal/permeability-increasing protein requires C/EBP epsilon.International journal of hematology · 2007Trial
- A novel CXCL8(3-72) K11R/G31P-BPIEmerging microbes & infections · 2026Article
- The dual functions of the GTPase BipA in ribosome assembly and surface structure biogenesis in Salmonella enterica serovar Typhimurium.PLoS pathogens · 2025Article
- Chimeric hBPIArchives of microbiology · 2025Article
- Bactericidal Permeability-Increasing Protein (BPI) InhibitsBiomolecules · 2024Article
- Subversion of a family of antimicrobial proteins byFrontiers in cellular and infection microbiology · 2024Article
- Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis.Marine drugs · 2023Review
- Article
- Bactericidal/Permeability-Increasing Protein Downregulates the Inflammatory Response in In Vivo Models of Arthritis.International journal of molecular sciences · 2022Article
- Differential Enhancement of Neutrophil Phagocytosis by Anti-Bactericidal/Permeability-Increasing Protein Antibodies.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Bactericidal/Permeability-Increasing Protein Preeminently Mediates Clearance ofFrontiers in immunology · 2021Article
- Killing three birds with one BPI: Bactericidal, opsonic, and anti-inflammatory functions.Journal of translational autoimmunity · 2021Review
- Low-Avidity Autoantibodies against Bactericidal/Permeability-Increasing Protein Occur in Gram-Negative and Gram-Positive Bacteremia.Infection and immunity · 2020Article
- Lipopolysaccharide (LPS)-binding protein stimulates CD14-dependent Toll-like receptor 4 internalization and LPS-induced TBK1-IKKϵ-IRF3 axis activation.The Journal of biological chemistry · 2018Article
- The Ontogeny of a Neutrophil: Mechanisms of Granulopoiesis and Homeostasis.Microbiology and molecular biology reviews : MMBR · 2018Review
- Bactericidal/Permeability-Increasing Protein Is an Enhancer of Bacterial Lipoprotein Recognition.Frontiers in immunology · 2018Article
- Article
- Age-Appropriate Functions and Dysfunctions of the Neonatal Neutrophil.Frontiers in pediatrics · 2017Review
- Importance of the residue 190 on bactericidal activity of the bactericidal/permeability-increasing protein 5.Oncotarget · 2016Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The host response to Gram-negative bacterial infection is influenced by two homologous lipopolysaccharide (LPS)-interactive proteins, LPS-binding protein (LBP) and the bacteridical/permeability-increasing protein (BPI). Both proteins bind LPS via their N-terminal domains but produce profoundly different effects: BPI and a bioactive N-terminal fragment BPI-21 exert a selective and potent antibacterial effect upon Gram-negative bacteria and suppress LPS bioactivity whereas LBP is not toxic toward Gram-negative bacteria and potentiates LPS bioactivity. The latter effect of LBP requires the C-terminal domain for delivery of LPS to CD14, so we postulated that the C-terminal region of BPI may serve a similar delivery function but to distinct targets. LBP, holoBPI, BPI-21, and LBP/BPI chimeras were compared for their ability to promote uptake by human phagocytes of an encapsulated, phagocytosis-resistant strain of Escherichia coli. We show that only bacteria preincubated with holoBPI are ingested by neutrophils and monocytes. These findings suggest that, when extracellular holoBPI is bound via its N-terminal domain to Gram-negative bacteria, the C-terminal domain promotes bacterial attachment to neutrophils and monocytes, leading to phagocytosis. Therefore, analogous to the role of the C-terminal domain of LBP in delivery of LPS to CD14, the C-terminal domain of BPI may fulfill a similar function in BPI-specific disposal pathways for Gram-negative bacteria.
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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.