Evidence map›Paper›PMID 42336997›Full record

ArticleCommunications biology2026

Cryo-EM structure of the native assembled Mfa type V pilus from the periodontal pathogen Porphyromonas gingivalis.

Satoshi Shibata, Hideyuki Matsunami, Kazuhisa Ouhara, Yuri Taniguchi, Makoto Tokoro Schreiber, Alejandro Villar-Brillones, Koji Nakayama, Mikio Shoji, Matthias Wolf

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Satoshi ShibataMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan. sshibata@tottori-u.ac.jp.ORCID http://orcid.org/0000-0002-6095-9796
Hideyuki MatsunamiMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.ORCID http://orcid.org/0000-0001-5814-3766
Kazuhisa OuharaDepartment of Periodontal Medicine, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
Yuri TaniguchiDepartment of Periodontal Medicine, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
Makoto Tokoro SchreiberMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.
Alejandro Villar-BrillonesIT Division, Institutional Applications, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.ORCID http://orcid.org/0000-0002-4246-3877
Koji NakayamaDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.ORCID http://orcid.org/0000-0001-7685-0042
Mikio ShojiDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.
Matthias WolfMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan. matthias.wolf@oist.jp.ORCID http://orcid.org/0000-0001-8480-0918

Funding

Japan Agency for Medical Research and Development (AMED) JP25ama121037MEXT | Japan Society for the Promotion of Science (JSPS) 20K06581MEXT | Japan Society for the Promotion of Science (JSPS) 23K006530MEXT | Japan Society for the Promotion of Science (JSPS) JP17K07318MEXT | Japan Society for the Promotion of Science (JSPS) JP19K10083
6 · The paper itself

Abstract

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 Å resolution. The atomic model of the Mfa1 filament reveals that Mfa1 pilins polymerize by protease-mediated strand exchange and retain a Ca

Indexed as

Cryoelectron MicroscopyFimbriae, BacterialFimbriae ProteinsPorphyromonas gingivalisBacterial ProteinsHumansModels, MolecularProtein ConformationBacterial ProteinsFimbriae ProteinsMfa1 protein, Porphyromonas gingivalis

Identifiers

PMID42336997
PMCPMC13655056

What OpenQuestion holds

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Registered trials

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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.