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Updated: Dec 11, 2025

Visualization of Twitching Motility and Characterization of the Role of the PilG in Xylella fastidiosa
Published on: April 8, 2016
Biogenesis of Type V pili.
Mikio Shoji1, Satoshi Shibata2, Takayuki Sueyoshi1
1Department of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.
Porphyromonas gingivalis pili, known as Type V pili, assemble via a novel protease-mediated mechanism. This study details their unique transport and assembly, distinct from other bacterial pili.
Area of Science:
- Microbiology
- Structural Biology
- Bacteriology
Background:
- Pili (fimbriae) are bacterial surface filaments.
- Porphyromonas gingivalis pili (Fim pili) have unique characteristics, including a larger stalk pilin (FimA).
- Previous work indicated FimA secretion as a lipoprotein precursor requiring protease processing for pilus formation.
Purpose of the Study:
- To elucidate the novel assembly and transport mechanisms of P. gingivalis Type V pili.
- To provide structural insights into Fim pili formation.
- To describe lipoprotein transport in Gram-negative bacteria.
Main Methods:
- Purification of pili from Porphyromonas gingivalis.
- Determination of crystal structures of FimA and related proteins.
- Cryoelectron microscopy of pilus structure.
Main Results:
- P. gingivalis Fim pili are formed via a protease-mediated strand-exchange mechanism.
- Cryo-EM data support this novel assembly pathway.
- Type V pili assembly differs significantly from other known pili.
- Surface lipoproteins like FimB are involved in Fim pili anchoring.
Conclusions:
- P. gingivalis Fim pili represent a distinct class, designated Type V pili, due to their unique assembly and transport mechanisms.
- Protease activity is crucial for Fim pili formation.
- Understanding these mechanisms offers insights into bacterial surface structure assembly and lipoprotein transport.
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