Porphyromonas gingivalis Proteinase-Adhesin Polyproteins of Gamma Interferon Mediated by Cysteine Complex Protein Expression by Human Modulation of Major Histocompatibility
نویسندگان
چکیده
منابع مشابه
Modulation of gamma interferon-induced major histocompatibility complex class II gene expression by Porphyromonas gingivalis membrane vesicles.
Gamma interferon (IFN-gamma)-induced endothelial cells actively participate in initiating immune responses by interacting with CD4(+) T cells via class II major histocompatibility complex (MHC) surface glycoproteins. Previously, Porphyromonas gingivalis membrane vesicles were shown to selectively inhibit IFN-gamma-induced surface expression of HLA-DR molecules by human umbilical cord vascular e...
متن کاملCharacterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes.
Porphyromonas gingivalis has been associated with the development of adult periodontitis and cysteine proteinases with Arg- and Lys-specific activity have been implicated as major virulence factors. In a cell sonicate of P. gingivalis W50, a complex of non-covalently associated proteins has been previously characterized. This complex is composed of a 45 kDa Arg-specific, calcium-stabilized cyst...
متن کاملThe K1K2 region of Lys-gingipain of Porphyromonas gingivalis blocks induction of HLA expression by gamma interferon.
In the context of periodontal disease, cysteine proteinases or gingipains from Porphyromonas gingivalis have been implicated in the hydrolysis of cytokines, including gamma interferon (IFN-γ). This cytokine plays a crucial role in host defenses, in part, by regulating expression of major histocompatibility complex molecules. Our recent analysis has identified three structurally defined modules,...
متن کاملHigh molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism.
Periodontal disease is an oral inflammatory disease affecting the supporting structures of teeth. Porphyromonas gingivalis, a major pathogenic agent for the disease, expresses a number of virulence factors, including cysteine proteases called the gingipains. The arginine- and lysine-specific gingipains, HRgpA and Kgp, respectively, are expressed as high molecular weight forms containing both ca...
متن کاملAn immune response directed to proteinase and adhesin functional epitopes protects against Porphyromonas gingivalis-induced periodontal bone loss.
Porphyromonas gingivalis, a pathogen associated with periodontitis, bound to fibrinogen, fibronectin, hemoglobin, and collagen type V with a similar profile to that of its major virulence factor, the cell surface RgpA-Kgp proteinase-adhesin complex. Using peptide-specific, purified Abs in competitive inhibition ELISAs and epitope mapping assays, we have identified potential adhesin binding moti...
متن کامل