Abstract
Periodontal inflammation is one of the most common chronic inflammatory conditions in humans. Despite recent advances in identifying and characterizing oral microbiota dysbiosis in the pathogenesis of gum disease, just how host factors maintain a healthy homeostatic oral microbial community or prevent the development of a pathogenic oral microbiota remains poorly understood. An important determinant of microbiota fate is local antimicrobial proteins. Here, we report that chemoattractant protein chemerin, which we recently identified as a potent endogenous antimicrobial agent in body barriers such as the skin, is present in the oral cavity under homeostatic and inflammatory conditions. Chemerin and a chemerin-derived antimicrobial peptide are bactericidal against select bacteria strategically positioned in dental biofilm. Gingival crevicular samples from patients with gingivitis but not periodontitis contain abundant bioactive chemerin capable of inducing CMKLR1-dependent leukocyte migration. Gingipains secreted by the periodontopathogen P. gingivalis inactivate chemerin. Together, these data suggest that as an antimicrobial agent and leukocyte chemoattractant, chemerin likely contributes to antimicrobial immune defense in the oral cavity.
Highlights
Chemerin is a chemoattractant protein implicated in recruitment of dendritic cells (DCs), macrophages, and NK cells to sites of inflammation [1]
To determine whether chemerin serves as antimicrobial peptides (AMPs) against oral bacteria, we first analyzed chemerin protein levels in saliva of healthy individuals with no signs of periodontal disease
We demonstrate that chemerin is expressed in the oral cavity, where it likely contributes to antibacterial defense as an antibacterial agent and as a chemoattractant for immune cells
Summary
Chemerin is a chemoattractant protein implicated in recruitment of dendritic cells (DCs), macrophages, and NK cells to sites of inflammation [1]. These immune cells express the G-protein-coupled signaling receptor CMKLR1, which mediates cell chemotactic responses to bioactive chemerin [2, 3]. Chemerin circulates as an inactive isoform (chemS163) and needs to be proteolytically processed to display chemotactic potential. Bioactive chemerin lacking six amino acids in the C-terminus (chemS157) has been isolated from body fluids [1], and various serine and cysteine proteases of host and microbial origin can generate active chemerin by C-terminal processing in vitro [4,5,6]. Chemerin is broadly expressed in numerous anatomic sites, including liver and fat tissues as well as by epithelial cells in the skin epidermis [7,8,9,10], intestinal epithelium [8, 11], and pulmonary
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
