Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens

Lee, Sung-Hoon; Jun, Hye‐Kyoung; Lee, Haeri; Chung, Chong-Pyoung; Choi, Bong‐Kyu

doi:10.1016/j.ijantimicag.2009.09.024

Cited by 78 publications

(69 citation statements)

References 34 publications

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“…Consequently, LPS is transferred to TLR by binding to LBP and CD14. LPS binds TLR2 or TLR4 according to the structure of acyl chain in lipid A (Lee et al, 2010), and induces inflammation via the intracellular signaling molecules of TLR (Akira and Takeda, 2004). PGN is composed of β-1,4-linked N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) cross-linked by short peptides.…”

Section: Introductionmentioning

confidence: 99%

Antagonistic effect of peptidoglycan of Streptococcus sanguinis on lipopolysaccharide of major periodontal pathogens

Lee

2015

J Microbiol.

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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.

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Section: Introductionmentioning

confidence: 99%

Antagonistic effect of peptidoglycan of Streptococcus sanguinis on lipopolysaccharide of major periodontal pathogens

Lee

2015

J Microbiol.

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“…A similar mechanism was suggested for P. gingivalis and Prevotella intermedia, which were found to be susceptible to cecropin B (derived from silk moth), despite their ability to cleave the peptide (17). T. forsythia is also susceptible to LL-37 (42,43) in spite of its high proteolytic capacity, including the presence of an active metalloproteinase (karylisin) capable of inactivating the antimicrobial activity of LL-37 (42).…”

Section: Figmentioning

confidence: 64%

The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor

2012

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Host defense peptides are innate immune effectors that possess both bactericidal activities and immunomodulatory functions. Deficiency in the human host defense peptide LL-37 has previously been correlated with severe periodontal disease. Treponema denticola is an oral anaerobic spirochete closely associated with the pathogenesis of periodontal disease. The T. denticola major surface protein (MSP), involved in adhesion and cytotoxicity, and the dentilisin serine protease are key virulence factors of this organism. In this study, we examined the interactions between LL-37 and T. denticola. The three T. denticola strains tested were susceptible to LL-37. Dentilisin was found to inactivate LL-37 by cleaving it at the Lys, Phe, Gln, and Val residues. However, dentilisin deletion did not increase the susceptibility of T. denticola to LL-37. Furthermore, dentilisin activity was found to be inhibited by human saliva. In contrast, a deficiency of the T. denticola MSP increased resistance to LL-37. The MSP-deficient mutant bound less fluorescently labeled LL-37 than the wild-type strain. MSP demonstrated specific, dose-dependent LL-37 binding. In conclusion, though capable of LL-37 inactivation, dentilisin does not protect T. denticola from LL-37. Rather, the rapid, MSPmediated binding of LL-37 to the treponemal outer sheath precedes cleavage by dentilisin. Moreover, in vivo, saliva inhibits dentilisin, thus preventing LL-37 restriction and ensuring its bactericidal and immunoregulatory activities.

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“…F. nucleatum ATCC 25586 and P. gingivalis ATCC 33277 were cultured anaerobically with BHI broth supplemented with hemin (1 mg/ml) and vitamin K (0.2 mg/ml) at 37∞C, anaerobically. T. forsythia ATCC 43037 and T. denticola ATCC 35405 were cultured in modified new oral spirochete (mNOS) broth (Lee et al, 2010) and tryptone-yeast extract-gelatin-volatile fatty acid-serum (TYGVS) broth respectively, at 37∞C (Ohta et al, 1986) in an anaerobic atmosphere.…”

Section: Methodsmentioning

confidence: 99%

Inhibitory effect of <i>Lactococcus lactis</i> on the bioactivity of periodontopathogens

Shin

Baek

Lee

2018

J. Gen. Appl. Microbiol.

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Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens

Cited by 78 publications

References 34 publications

Antagonistic effect of peptidoglycan of Streptococcus sanguinis on lipopolysaccharide of major periodontal pathogens

Antagonistic effect of peptidoglycan of Streptococcus sanguinis on lipopolysaccharide of major periodontal pathogens

The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor

Inhibitory effect of <i>Lactococcus lactis</i> on the bioactivity of periodontopathogens

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