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Infection and Immunity, December 2009, p. 5558-5563, Vol. 77, No. 12
0019-9567/09/$08.00+0 doi:10.1128/IAI.00648-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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Stella Chaushu,2,
Daniela Balter,1 and
Gilad Bachrach1*
Institute of Dental Sciences,1 Department of Orthodontics, Hebrew University-Hadassah School of Dental Medicine, Jerusalem, Israel2
Received 8 June 2009/ Returned for modification 6 July 2009/ Accepted 19 September 2009
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 of 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 and 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.
Published ahead of print on 5 October 2009.
The authors have paid a fee to allow immediate free access to this article.
These authors contributed equally to the study.
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