Recombinant Porphyromonas gingivalis Major fimbrium subunit FimA type-1 (fimA)

Function

Structural subunit of the major fimbriae. These long, 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:12593606, PubMed:15165251, PubMed:17526848, PubMed:17675496, PubMed:20530728, PubMed:27062925, PubMed:9786913). They play an important role in the invasion of periodontal tissues (PubMed:12593606). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification (PubMed:23809984). The sequence-based classification correlates with pathogenicity (PubMed:17675496)

Subcellular Location

Fimbrium; Cell outer membrane

Subunit

Fimbriae are composed of a major, structural subunit (FimA) and the minor components FimC, FimD and FimE (PubMed:17526848, PubMed:17675496). Head-to-tail oligomerization of FimA molecules mediates assembly of the fimbrium stalk, while the minor components probably form the fimbrium tip. Linear, head-to-tail oligomerization of FimA is mediated by a conformation change, facilitating the insertion of a C-terminal beta-strand into a groove in the N-terminal domain of the following subunit (By similarity). The anchoring subunit FimB limits fimbrium length and is important for solid fimbrium attachment to the outer membrane. In its absence, the major fimbriae become very long and are easily detached from the membrane (PubMed:27062925)

• Fujiwara T. et al. Molecular cloning and sequencing of the fimbrilin gene of Porphyromonas gingivalis strains and characterization of recombinant proteins. — Biochem. Biophys. Res. Commun. (1993)
• Naito M. et al. Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis. — DNA Res. (2008)
• Onoe T. et al. Identification of Porphyromonas gingivalis prefimbrilin possessing a long leader peptide: possible involvement of trypsin-like protease in fimbrilin maturation. — Microb. Pathog. (1995)
• Kadowaki T. et al. Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. — J. Biol. Chem. (1998)
• Xie H. et al. Promoter architecture of the Porphyromonas gingivalis fimbrillin gene. — Infect. Immun. (1999)
• Umemoto T. et al. Characterization of biologically active cell surface components of a periodontal pathogen. The roles of major and minor fimbriae of Porphyromonas gingivalis. — J. Periodontology (2003)
• Shoji M. et al. The major structural components of two cell surface filaments of Porphyromonas gingivalis are matured through lipoprotein precursors. — Mol. Microbiol. (2004)
• Wang M. et al. Fimbrial proteins of porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and complement receptor 3 to persist in macrophages. — J. Immunol. (2007)