Porphyromonas gingivalis fimbriae and their synthetic peptides induce proinflammatory cytokines in human peripheral blood monocyte cultures.
Porphyromonas gingivalis fimbriae as well as synthetic peptides that mimic the fimbrial subunit protein, which includes the amino acid sequence XLTXXLTXXNXX, induced high production of proinflammatory cytokines such as interleukin-1 beta, interleukin-6, interleukin-8, tumor necrosis factor-alpha in human peripheral blood monocyte/macrophage cultures. Responses induced by some peptide segments were comparable to those induced by Escherichia coli lipopolysaccharides. A chemically modified peptide analogous to an active peptide segment was found to be antagonistic with regard to interleukin-6 production induced by the native fimbriae. It may be suggested that P. gingivalis fimbriae and their degraded peptides function as proinflammatory agents in vivo, while certain analog peptides inhibited the process.
Ogawa
T
T
Department of Oral Microbiology, Osaka University Faculty of Dentistry, Japan.
Uchida
H
H
Hamada
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000276:immunology*; D002478:Cells, Cultured; D016207:Cytokines / Q000096:biosynthesis*; D004797:Enzyme-Linked Immunosorbent Assay; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000276:immunology*; D006801:Humans; D008264:Macrophages / Q000276:immunology; D008969:Molecular Sequence Data; D009000:Monocytes / Q000276:immunology; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology*; D016966:Porphyromonas gingivalis / Q000276:immunology*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D016207:Cytokines; D010446:Peptide Fragments; C063055:fimbrillin; D036781:Fimbriae Proteins