| Structural highlights
Function
MFA1_PORG3 Structural subunit of the minor fimbriae (PubMed:12593606, PubMed:19589838, PubMed:24118823). These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:11083792, PubMed:12593606, PubMed:15972485, PubMed:19589838, PubMed:23809984, PubMed:24118823, PubMed:26001707, PubMed:26437277). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Mfa1 orthologs from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).[1] [2] [3] [4] [5] [6] [7] [8]
Publication Abstract from PubMed
Porphyromonas gingivalis is a primary pathogen causing periodontal disease. The cell has two kinds of type V pili, the Fim pilus and the Mfa pilus, both of which play essential roles in colonization, biofilm formation, and pathogenicity. The functional polymerized structure of the Fim pilus is known, whereas the structure and assembly mechanism of the Mfa pilus remain unclear. Here, we show the structure of the polymerized recombinant Mfa1 stalk pilin determined by cryo-electron microscopy at 3.0 A resolution. The atomic model of the Mfa1 filament reveals that Mfa1 pilins polymerize by protease-mediated strand exchange and retain a Ca(2+) ion in the metal-binding pocket, which modulates immune recognition of the Mfa pilus by human cells. Furthermore, we elucidated the three-dimensional architecture of the streptococcal-binding region on the Mfa pilus. Our results further strengthen evidence that protease-mediated strand exchange is the universal assembly mechanism of type V pili. Our structure of the polymerized Mfa pilus, which represents the functional state on the cell surface, provides targets for antimicrobial drug design to treat periodontal disease and P. gingivalis-related systemic diseases.
Cryo-EM structure of the native assembled Mfa type V pilus from the periodontal pathogen Porphyromonas gingivalis.,Shibata S, Matsunami H, Ouhara K, Taniguchi Y, Schreiber MT, Villar-Brillones A, Nakayama K, Shoji M, Wolf M Commun Biol. 2026 Jun 24. doi: 10.1038/s42003-026-10515-2. PMID:42336997[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chung WO, Demuth DR, Lamont RJ. Identification of a Porphyromonas gingivalis receptor for the Streptococcus gordonii SspB protein. Infect Immun. 2000 Dec;68(12):6758-62. PMID:11083792
- ↑ Umemoto T, Hamada N. Characterization of biologically active cell surface components of a periodontal pathogen. The roles of major and minor fimbriae of Porphyromonas gingivalis. J Periodontol. 2003 Jan;74(1):119-22. doi: 10.1902/jop.2003.74.1.119. PMID:12593606 doi:https://dx.doi.org/10.1902/jop.2003.74.1.119
- ↑ Park Y, Simionato MR, Sekiya K, Murakami Y, James D, Chen W, Hackett M, Yoshimura F, Demuth DR, Lamont RJ. Short fimbriae of Porphyromonas gingivalis and their role in coadhesion with Streptococcus gordonii. Infect Immun. 2005 Jul;73(7):3983-9. doi: 10.1128/IAI.73.7.3983-3989.2005. PMID:15972485 doi:https://dx.doi.org/10.1128/IAI.73.7.3983-3989.2005
- ↑ Hasegawa Y, Iwami J, Sato K, Park Y, Nishikawa K, Atsumi T, Moriguchi K, Murakami Y, Lamont RJ, Nakamura H, Ohno N, Yoshimura F. Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2. Microbiology. 2009 Oct;155(Pt 10):3333-47. doi: 10.1099/mic.0.028928-0. Epub 2009, Jul 9. PMID:19589838 doi:https://dx.doi.org/10.1099/mic.0.028928-0
- ↑ Nagano K, Abiko Y, Yoshida Y, Yoshimura F. Genetic and antigenic analyses of Porphyromonas gingivalis FimA fimbriae. Mol Oral Microbiol. 2013 Oct;28(5):392-403. doi: 10.1111/omi.12032. Epub 2013 Jul, 1. PMID:23809984 doi:https://dx.doi.org/10.1111/omi.12032
- ↑ Hasegawa Y, Nagano K, Ikai R, Izumigawa M, Yoshida Y, Kitai N, Lamont RJ, Murakami Y, Yoshimura F. Localization and function of the accessory protein Mfa3 in Porphyromonas gingivalis Mfa1 fimbriae. Mol Oral Microbiol. 2013 Dec;28(6):467-80. doi: 10.1111/omi.12040. Epub 2013 Oct , 5. PMID:24118823 doi:https://dx.doi.org/10.1111/omi.12040
- ↑ Nagano K, Hasegawa Y, Yoshida Y, Yoshimura F. A Major Fimbrilin Variant of Mfa1 Fimbriae in Porphyromonas gingivalis. J Dent Res. 2015 Aug;94(8):1143-8. doi: 10.1177/0022034515588275. Epub 2015 May, 22. PMID:26001707 doi:https://dx.doi.org/10.1177/0022034515588275
- ↑ Ikai R, Hasegawa Y, Izumigawa M, Nagano K, Yoshida Y, Kitai N, Lamont RJ, Yoshimura F, Murakami Y. Mfa4, an Accessory Protein of Mfa1 Fimbriae, Modulates Fimbrial Biogenesis, Cell Auto-Aggregation, and Biofilm Formation in Porphyromonas gingivalis. PLoS One. 2015 Oct 5;10(10):e0139454. doi: 10.1371/journal.pone.0139454., eCollection 2015. PMID:26437277 doi:https://dx.doi.org/10.1371/journal.pone.0139454
- ↑ Shibata S, Matsunami H, Ouhara K, Taniguchi Y, Schreiber MT, Villar-Brillones A, Nakayama K, Shoji M, Wolf M. Cryo-EM structure of the native assembled Mfa type V pilus from the periodontal pathogen Porphyromonas gingivalis. Commun Biol. 2026 Jun 24. PMID:42336997 doi:10.1038/s42003-026-10515-2
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