ArticleInfection and immunity2000
Identification of a human lactoferrin-binding protein in Gardnerella vaginalis.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 20 citations in OpenAlex.
- Vaginal pharmacomicrobiomics modulates risk of persistent and recurrent bacterial vaginosis.NPJ biofilms and microbiomes · 2025Review
- Cargo exchange between human and bacterial extracellular vesicles in gestational tissues: a new paradigm in communication and immune development.Extracellular vesicles and circulating nucleic acids · 2024Review
- Antimicrobial activity of bovine lactoferrin againstFrontiers in microbiology · 2022Article
- Mucosal lactoferrin response to genital tract infections is associated with iron and nutritional biomarkers in young Burkinabé women.European journal of clinical nutrition · 2019Article
- Influence of iron status on risk of maternal or neonatal infection and on neonatal mortality with an emphasis on developing countries.Nutrition reviews · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have shown that Gardnerella vaginalis can utilize iron-loaded human lactoferrin as a sole source of iron. In this study, G. vaginalis cells were shown to bind digoxigenin (DIG)-labeled human lactoferrin in a dot blot assay. Using the DIG-labeled human lactoferrin, a 120-kDa human lactoferrin-binding protein was detected by Western blot analysis of G. vaginalis proteins. The lactoferrin-binding activity of this protein was found to be heat stable. Competition studies indicated that this binding activity was specific for human lactoferrin. Treatment of G. vaginalis cells with proteases suggested that this protein was surface exposed. An increase in lactoferrin binding by the 120-kDa protein was observed in G. vaginalis cells grown under iron-restrictive conditions, suggesting that this activity may be iron regulated.
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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.