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| Kofi... |
 Posted: Thu Oct 29, 2009 8:38 pm |
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Infect Immun. 2009 Oct 5;
Saliva enables the antimicrobial activity of LL-37 in the presence of
proteases of Porphyromonas gingivalis.
Gutner M, Chaushu S, Balter D, Bachrach G.
Institute of Dental Sciences, and Department of Orthodontics, the Hebrew
University-Hadassah School of Dental Medicine, Jerusalem, Israel.
Proteolysis is a common microbial virulence mechanism that enables the
destruction of host tissue and evasion from host defense mechanisms.
Antimicrobial peptides, also known as host defense peptides are effector
molecules of the innate immunity that demonstrate a broad range of
antimicrobial and immunoregulatory activities. Deficiency in the human
LL-37 antimicrobial peptide was previously correlated with severe
periodontal disease. Porphyromonas gingivalis, the major pathogen
associated with periodontitis is highly proteolytic. In this study P.
gingivalis was found capable of degrading LL-37 by utilizing its
arginine specific gingipains. Saliva collected from volunteers with a
healthy periodontium protected LL-37 from proteolysis by P. gingivalis.
Salivary protection of LL-37 was heat resistant, specific, and enabled
LL-37 to inhibit growth of Escherichia coli in the presence of the P.
gingivalis proteases. Previously, saliva and other body fluids have been
shown to inhibit the antimicrobial activity of LL-37. Here we
demonstrate that at a cost of a small reduction in the bactericidal
activity of LL-37, saliva enables the antibacterial activity of LL-37
despite the presence of proteases secreted by the main
periodontopathogen.
PMID: 19805540 |
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