ArticleInfection and immunity2005
Short fimbriae of Porphyromonas gingivalis and their role in coadhesion with Streptococcus gordonii.
Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 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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Who cites it
127 citing papers in PubMed, 185 citations in OpenAlex.
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- Insights into the enigma of oral streptococci in carcinogenesis.Microbiology and molecular biology reviews : MMBR · 2024Review
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- Phages are unrecognized players in the ecology of the oral pathogen Porphyromonas gingivalis.Microbiome · 2023Article
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- Local and Systemic Effects ofMicroorganisms · 2023Review
- Bacterial biofilms in the human body: prevalence and impacts on health and disease.Frontiers in cellular and infection microbiology · 2023Review
- Structural and antigenic characterization of a novel genotype of Mfa1 fimbriae inJournal of oral microbiology · 2023Article
- Current concepts in the pathogenesis of periodontitis: from symbiosis to dysbiosis.Journal of oral microbiology · 2023Review
67 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 6 institutions in 3 countries.
Funding
Abstract
Porphyromonas gingivalis, one of the causative agents of adult periodontitis, attaches and forms biofilms on substrata of Streptococcus gordonii. Coadhesion and biofilm development between these organisms requires the interaction of the short fimbriae of P. gingivalis with the SspB streptococcal surface polypeptide. In this study we investigated the structure and binding activities of the short fimbriae of P. gingivalis. Electron microscopy showed that isolated short fimbriae have an average length of 103 nm and exhibit a helical structure with a pitch of ca. 27 nm. Mfa1, the major protein subunit of the short fimbriae, bound to SspB protein, and this reaction was inhibited by purified recombinant Mfa1 and monospecifc anti-Mfa1 serum in a dose-dependent manner. Complementation of a polar Mfa1 mutant with the mfa1 gene restored the coadhesion phenotype of P. gingivalis. Hence, the Mfa1 structural fimbrial subunit does not require accessory proteins for binding to SspB. Furthermore, the interaction of Mfa1 with SspB is necessary for optimal coadhesion between P. gingivalis and S. gordonii.
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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.