Fimbriae of Porphyromonas gingivalis are filamentous appendages on the cell surface and are thought to be one of the virulence factors. The fimA gene encoding the subunit protein of fimbriae, fimbrillin (FimA), was classified into four typeable variants (types I to IV). We previously examined the distribution of P. gingivalis in terms of fimA genotypes in periodontitis patients using a fimA typ...

Porphyromonas gingivalis fimbriae are an important virulence factor involved in attachment and invasion. Fimbrillin, encoded by the fimA gene, is the major subunit protein of the fimbriae. To elucidate the influence of environmental signals on the expression of the fimA gene, a strain of P. gingivalis (designated PLE) containing a chromosomal transcriptional fusion between a promoterless lacZ g...

This study documents the presence of type 1 fimbriae on Shigella and confirms these mannose-sensitive adherence structures to be bona fide components of the Shigella surface. While laboratory-passaged Shigella strains and lyophilized clinical isolates failed to express type 1 fimbriae, 6 of 20 recent clinical isolates, including 4 Shigella flexneri strains, 1 Shigella boydii strain, and 1 Shige...

Cysteine proteases, including Arg-gingipain of Porphyromonas gingivalis, have been implicated as important virulence factors in periodontal diseases. These enzymes are also involved in the hemagglutinating activity of the organisms. In order to determine the role of proteases in the colonization of the gingival margin, we have compared the attachment properties of P. gingivalis 381 with those o...

Fimbriae of Porphyromonas gingivalis, a periodontopathogen, play an important role in its adhesion to and invasion of host cells. The fimA genes encoding fimbrillin (FimA), a subunit protein of fimbriae, have been classified into five types, types I to V, based on nucleotide sequences. We previously reported that P. gingivalis with type II fimA was strongly associated with adult periodontitis. ...

Porphyromonas gingivalis 381 fimbriae, their synthetic peptide segments, and lipopolysaccharide (LPS) were examined for hemagglutinating and migration-stimulating activities. P. gingivalis 381 fimbriae clearly caused hemagglutination, and several oligopeptide segments such as FP381(61-80), FP381(171-185), and FP381(302-321), corresponding to the amino acid residue numbers based on the amino aci...