ArticleInfection and immunity2004
PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin [corrected].
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 98 papers.
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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.
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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
98 citing papers in PubMed.
- Review
- 3' UTR-mediated regulation of a protein chaperone by the pspA mRNA in Streptococcus pneumoniae.Nucleic acids research · 2026Article
- The Case for Pneumococcal Surface Protein A (PspA): A Comprehensive Review of a Leading Candidate in Pneumococcal Vaccine Research.Vaccines · 2026Review
- Capsule and PspA Cooperatively Confer Resistance ofInternational journal of molecular sciences · 2026Article
- Future Pneumococcal Vaccines: Shifting from Capsular Polysaccharides to Protein-Based Immunogens.Vaccines · 2026Review
- Antimicrobial Peptides Against Antimicrobial-Resistant Bacteria: Focus on Machine Learning.Infection and drug resistance · 2026Review
- In silico design and characterization of a novel multi-epitope mRNA vaccine candidate against Streptococcus pneumoniae.Scientific reports · 2025Article
- Novel processes to obtain pneumococcal surface proteins for vaccines.Applied microbiology and biotechnology · 2025Review
- Intranasal influenza-vectored vaccine expressing pneumococcal surface protein A protects against Influenza and Streptococcus pneumoniae infections.NPJ vaccines · 2024Article
- Pneumococcal surface protein A (PspA) prevents killing of Streptococcus pneumoniae by indolicidin.Scientific reports · 2024Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Novel method for production and purification of untagged pneumococcal surface protein A from clade 1.Applied microbiology and biotechnology · 2024Article
- Article
- Naturally acquired antibodies against 4 Streptococcus pneumoniae serotypes in Pakistani adults with type 2 diabetes mellitus.PloS one · 2024Article
- An immunoinformatics approach to epitope-based vaccine design against PspA in Streptococcus pneumoniae.Journal, genetic engineering & biotechnology · 2023Article
- Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.Pharmaceutics · 2023Review
- Phage Display-Derived Peptides and Antibodies for Bacterial Infectious Diseases Therapy and Diagnosis.Molecules (Basel, Switzerland) · 2023Review
- Immunoinformatics-aided design of a new multi-epitope vaccine adjuvanted with domain 4 of pneumolysin against Streptococcus pneumoniae strains.BMC bioinformatics · 2023Article
- Article
- Role ofFrontiers in cellular and infection microbiology · 2023Review
38 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoferrin is an important component of innate immunity through its sequestration of iron, bactericidal activity, and immune modulatory activity. Apolactoferrin (ALF) is the iron-depleted form of lactoferrin and is bactericidal against pneumococci and several other species of bacteria. We observed that lactoferricin (LFN), an 11-amino-acid peptide from the N terminus of lactoferrin, is bactericidal for Streptococcus pneumoniae. Strains of S. pneumoniae varied in their susceptibility to ALF. Lactoferrin is bound to the pneumococcal surface by pneumococcal surface protein A (PspA). Using mutant PspA(-) pneumococci of four different strains, we observed that PspA offers significant protection against killing by ALF. Knockout mutations in genes for two other choline-binding proteins (PspC and PcpA) did not affect killing by ALF. PspA did not have to be attached to the bacterial surface to inhibit killing, because the soluble recombinant N-terminal half of PspA could prevent killing by both ALF and LFN. An 11-amino-acid fragment of PspA was also able to reduce the killing by LFN. Antibody to PspA enhanced killing by lactoferrin. These findings suggested that the binding of ALF to PspA probably blocks the active site(s) of ALF that is responsible for killing.
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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.