FimB regulates FimA fimbriation in Porphyromonas gingivalis.
The periodontitis-associated pathogen Porphyromonas gingivalis colonizes and forms a biofilm in gingival crevices through fimbriae. It is known that the often-used strains ATCC 33277 and 381 produce long FimA fimbriae. We found a possible nonsense mutation within fimB, immediately downstream from fimA, coding a major subunit of FimA fimbriae of the strains. Indeed, P. gingivalis strains, except for ATCC 33277 and 381, universally expressed FimB, the gene product of fimB. Electron micrographs revealed that a FimB-restored strain had short and dense, "toothbrush"-like, FimA fimbriae. FimA overexpression elongated the fimbriae, whereas FimB overexpression shortened them. FimB restoration increased production of FimA and its accessory proteins. Thus, FimB regulates the length and expression of FimA fimbriae. Additionally, FimB restoration significantly reduced the release of FimA fimbriae from the cell surface, suggesting that FimB functions as an anchor of the fimbriae. The restoration enhanced adherent activity as well.
Department of Microbiology, School of Dentistry, Aichi-Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, Aichi 464-8650, Japan. nagano@dpc.agu.ac.jp
K
K
Nagano
Y
Y
Hasegawa
Y
Y
Murakami
S
S
Nishiyama
F
F
Yoshimura
D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology; D036781:Fimbriae Proteins / Q000235:genetics / Q000502:physiology*; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000378:metabolism*; D016966:Porphyromonas gingivalis / Q000235:genetics / Q000502:physiology*; D013045:Species Specificity
C063055:fimbrillin; D036781:Fimbriae Proteins