title: Antagonistic effect of peptidoglycan of Streptococcus sanguinis on lipopolysaccharide of major periodontal pathogens.
abstract: Streptococcus sanguinis is often found in subgingival biofilm including periodontopathogens, and is correlated with a delay in colonization by periodontopathogens. However, the effect of S. sanguinis on inflammation induced by periodontopathogens is poorly understood. Thus, this study investigated the effect of S. sanguinis peptidoglycan (PGN) on induction of TNF-α, IL-6, and IL-8 expression by lipopolysaccharide (LPS) of periodontal pathogens. LPS was extracted from Aggregatibacter actinomycetemcomitans, Porphyromonas gingivalis, and Tannerella forsythia, and PGN was isolated from S. sanguinis. THP-1 cells, a monocytic cell-line, were cotreated with LPS of the periodontal pathogens and S. sanguinis PGN, and then the expression of inflammatory cytokines was analyzed by real-time RT-PCR. To analyze the underlying mechanism, the binding assay of the LPS to CD14 or LPS-binding protein (LBP) was performed in the presence or absence of the PGN after coating recombinant human CD14 and LBP on EIA plate. The PGN inhibited the binding of LPS to CD14 and LBP in a dose-dependent manner. Also, THP-1 cells were co-treated with the LPS in the presence of N-acetylmuramic acid and N-acetylglucosamine, as components of PGN, and the competition binding assay to CD14 and LBP was performed. N-acetylmuramic acid inhibited the induction of inflammatory cytokine expression by LPS and the binding of LPS to CD14 or LBP whereas N-acetylglucosamine did not show such effect. Collectively, the results suggest that S. sanguinis PGN inhibited the cytokine expression induced by the LPS of periodontopathogens due to the inhibition of LPS binding to LBP and CD14. N-acetylmuramic acid of PGN may play a role in inhibition of the LPS binding of periodontopathogens to CD14 and LBP.
authors.affiliation: Department of Oral Microbiology and Immunology, College of Dentistry, Dankook University, Cheonan, 330-714, Republic of Korea, dennisyi@dankook.ac.kr.
authors.forename: Sung-Hoon
authors.initials: SH
authors.lastname: Lee
mesh_terms: D000209:Acute-Phase Proteins / Q000378:metabolism; D016976:Aggregatibacter actinomycetemcomitans / Q000737:chemistry / Q000378:metabolism / Q000472:pathogenicity; D002352:Carrier Proteins / Q000378:metabolism; D002460:Cell Line; D016207:Cytokines / Q000378:metabolism; D006801:Humans; D008070:Lipopolysaccharides / Q000037:antagonists & inhibitors*; D008562:Membrane Glycoproteins / Q000378:metabolism; D009000:Monocytes / Q000187:drug effects; D016871:Pasteurellaceae Infections / Q000382:microbiology / Q000517:prevention & control*; D010457:Peptidoglycan / Q000008:administration & dosage / Q000378:metabolism*; D016966:Porphyromonas gingivalis / Q000737:chemistry / Q000378:metabolism / Q000472:pathogenicity; D013298:Streptococcus sanguis / Q000378:metabolism*; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D002352:Carrier Proteins; D016207:Cytokines; D008070:Lipopolysaccharides; D008562:Membrane Glycoproteins; D010457:Peptidoglycan; D000099231:Lipopolysaccharide-Binding Protein