Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease.
Gingipains are the major cysteine proteinases synthesized by Porphyromonas gingivalis which, in soluble form, are able to initially convert IL-8 (77 amino acid residues) to a more potent species truncated at the amino terminus, followed by slow degradation and destruction of chemokine biological activity. In contrast, the same enzymes when associated with bacterial outer-membrane blebs (vesicles), instantly degrade this chemokine. This division of enhancing and inactivating activity between soluble and membrane-bound gingipains can cause the compartmentalization of pro- and anti-inflammatory reactions to distal and proximal positions from bacterial plaque, respectively, which may explain why, despite the massive neutrophil accumulation at periodontitis sites, there is no elimination of infection.
Mikolajczyk-Pawlinska
J
J
Department of Microbiology and Immunology, Institute of Molecular Biology, Jagiellonian University, Krakow, Poland.
Travis
J
J
Potempa
J
J
D018829:Adhesins, Bacterial; D003546:Cysteine Endopeptidases / Q000502:physiology*; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D016209:Interleukin-8 / Q000378:metabolism*; D018375:Neutrophil Activation; D009504:Neutrophils / Q000276:immunology*; D010447:Peptide Hydrolases / Q000378:metabolism; D010510:Periodontal Diseases / Q000276:immunology* / Q000382:microbiology; D016966:Porphyromonas gingivalis / Q000201:enzymology / Q000276:immunology* / Q000472:pathogenicity; D011994:Recombinant Proteins / Q000378:metabolism
D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D016209:Interleukin-8; D011994:Recombinant Proteins; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases