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• W2044292829 abstract "Tannerella forsythia is a gram-negative bacterium strongly associated with the development and/or progression of periodontal disease. Here, we have shown that a newly characterized matrix metalloprotease-like enzyme, referred to as karilysin, efficiently cleaved the antimicrobial peptide LL-37, significantly reducing its bactericidal activity. This may contribute to the resistance of T. forsythia to the antibacterial activity of LL-37, since their vitality was found not to be affected by LL-37 at concentrations up to 2.2 muM. Furthermore, proteolysis of LL-37 by karilysin not only abolished its ability to bind lipopolysaccharide (LPS) to quench endotoxin-induced proinflammatory activity, but LL-37 cleavage also caused the release of active endotoxin from the LPS/LL-37 complex. Proteolytic inactivation of LL-37 bactericidal activity by karilysin may protect LL-37-sensitive species in the subgingival plaque and maintain the local inflammatory reaction driven by LPS from gram-negative bacteria. Consequently, the karilysin protease may directly contribute to periodontal tissue damage and the development and/or progression of chronic periodontitis." @default.
• W2044292829 created "2016-06-24" @default.
• W2044292829 creator A5020083442 @default.
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• W2044292829 date "2010-01-01" @default.
• W2044292829 modified "2023-10-16" @default.
• W2044292829 title "Proteolytic Inactivation of LL-37 by Karilysin, a Novel Virulence Mechanism of <i>Tannerella forsythia</i>" @default.
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• W2044292829 doi "https://doi.org/10.1159/000281881" @default.
• W2044292829 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2956017" @default.
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