ArticleCommunications biology2021
Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 24 citations in OpenAlex.
- Cryo-EM structure of the native assembled Mfa type V pilus from the periodontal pathogen Porphyromonas gingivalis.Communications biology · 2026Article
- Identification of a LolB-like protein in Porphyromonas gingivalis reveals selective LolA-LolB pairing.Scientific reports · 2026Article
- Periodontitis and Chronic Liver Disease: Mechanistic Insights Focusing onMicroorganisms · 2026Review
- Oxidative Stress ReshapesAntibiotics (Basel, Switzerland) · 2026Article
- Fimbriae potentiateCurrent research in microbial sciences · 2026Review
- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- Megaplasmids associate withbioRxiv : the preprint server for biology · 2025Article
- Macrophages immunomodulation induced by Porphyromonas gingivalis and oral antimicrobial peptides.Odontology · 2023Review
- Structural and antigenic characterization of a novel genotype of Mfa1 fimbriae inJournal of oral microbiology · 2023Article
- Identification of a prototype human gutFrontiers in microbiology · 2023Article
- Porphyromonas gingivalis Virulence Factors and Clinical Significance in Periodontal Disease and Coronary Artery DiseasesPathogens (Basel, Switzerland) · 2022Review
- Cortisol Promotes Surface Translocation ofPathogens (Basel, Switzerland) · 2022Article
- Review
- Diversity analysis of genes encoding Mfa1 fimbrial components in Porphyromonas gingivalis strains.PloS one · 2021Article
- Fractionated ethanolic red ginger extract as antibacterial agent againstJournal of oral biology and craniofacial researchArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gram-negative bacterium Porphyromonas gingivalis is a secondary colonizer of the oral biofilm and is involved in the onset and progression of periodontitis. Its fimbriae, of type-V, are important for attachment to other microorganisms in the biofilm and for adhesion to host cells. The fimbriae are assembled from five proteins encoded by the mfa1 operon, of which Mfa5 is one of the ancillary tip proteins. Here we report the X-ray structure of the N-terminal half of Mfa5, which reveals a von Willebrand factor domain and two IgG-like domains. One of the IgG-like domains is stabilized by an intramolecular isopeptide bond, which is the first such bond observed in a Gram-negative bacterium. These features make Mfa5 structurally more related to streptococcal adhesins than to the other P. gingivalis Mfa proteins. The structure reported here indicates that horizontal gene transfer has occurred among the bacteria within the oral biofilm.
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