Anti-Inflammatory Activity of Antimicrobial Peptide Allomyrinasin Derived from the Dynastid Beetle, Allomyrina dichotoma
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In a previous work, we performed de novo RNA sequencing of Allomyrina dichotoma using next generation sequencing and identified several antimicrobial peptide candidates based on transcriptome analysis. Among them, a cationic antimicrobial peptide, allomyrinasin, was selected bioinformatically based on its physicochemical properties. Here, we assessed the antimicrobial and anti-inflammatory activities of allomyrinasin against microorganisms and mouse macrophage Raw264.7 cells. Allomyrinasin showed antimicrobial activities against various microbes and decreased the nitric oxide production of the lipopolysaccharide-induced Raw264.7 cells. Furthermore, quantitative RT-PCR and ELISA revealed that allomyrinasin reduced cytokine expression levels in the Raw264.7 cells. We also identified inducible nitric oxide synthase, cyclooxygenase-2 expression, and PGE2 production through western blot analysis and ELISA. We confirmed that allomyrinasin bound to bacterial cell membranes via a specific interaction with lipopolysaccharides. Taken together, these data indicate that allomyrinasin has antimicrobial and anti-inflammatory activities as exemplified in lipopolysaccharide-induced Raw264.7 cells. We have provided a potentially useful antimicrobial peptide candidate that has both antimicrobial and anti-inflammatory activities.
Abstract
In a previous work, we performed de novo RNA sequencing of Allomyrina dichotoma using next generation sequencing and identified several antimicrobial peptide candidates based on transcriptome analysis. Among them, a cationic antimicrobial peptide, allomyrinasin, was selected bioinformatically based on its physicochemical properties. Here, we assessed the antimicrobial and anti-inflammatory activities of allomyrinasin against microorganisms and mouse macrophage Raw264.7 cells. Allomyrinasin showed antimicrobial activities against various microbes and decreased the nitric oxide production of the lipopolysaccharide-induced Raw264.7 cells. Furthermore, quantitative RT-PCR and ELISA revealed that allomyrinasin reduced cytokine expression levels in the Raw264.7 cells. We also identified inducible nitric oxide synthase, cyclooxygenase-2 expression, and PGE2 production through western blot analysis and ELISA. We confirmed that allomyrinasin bound to bacterial cell membranes via a specific interaction with lipopolysaccharides. Taken together, these data indicate that allomyrinasin has antimicrobial and anti-inflammatory activities as exemplified in lipopolysaccharide-induced Raw264.7 cells. We have provided a potentially useful antimicrobial peptide candidate that has both antimicrobial and anti-inflammatory activities.
참고문헌 (29)
- Taketa K, "Allomyrina dichotoma lectin-nonreactive a-fetoprotein in hepatocellular carcinoma and other tumors : comparison with Ricinus communis agglutinin-1", Cancer Lett, 31, pp.325~331 (1986)
- Jeune KH, "Immunomodulating effect of the lectin from Allomyrina dichotoma", Korean J. Pharmacognosy, 32, pp.31~38 (2001)
- 정미연, "Anti‐obesity effect of Allomyrina dichotoma (Arthropoda: Insecta) larvae ethanol extract on 3T3‐L1 adipocyte differentiation", Entomological Research, 44(1), pp.9~16 (2014), 한국곤충학회
- Yoon YI, "Allomyrina dichotoma(Arthropoda : Insecta)larvae confer resistance to obesity in mice fed a high-fat diet", Nutrients, 7, pp.1978~1991 (2015)
- Kim J, "Allomyrina dichotoma larvae regulate food intake and body weight in high fat diet-induced obese mice through mTOR and Mapk signaling pathways", Nutrients, 8, pp.100~ (2016)
- 김민지, "Effects of solvent fractions of Allomyrina dichotoma larvae through the inhibition of in vitro BACE1 and β‐amyloid(25–35)‐induced toxicity in rat pheochromocytoma PC12 cells", Entomological Research, 44(1), pp.23~30 (2014), 한국곤충학회
- 최용화, "장수풍뎅이 유충 추출물이 사염화탄소에 의한 마우스의 간 손상에 미치는 영향", 한국식품영양과학회지, 35(10), pp.1349~1355 (2006), 한국식품영양과학회
- 김덕성, "Allomyrina Dichotoma Larva추출물이 췌장베타세포에서 streptozotocin에 의해 유도된 산화적 손상에 대한 보호효과", 환경독성보건학회지, 22(4), pp.349~355 (2007), 환경독성보건학회
- 이경진, "Protective Effect of Allomyrina dichotoma Larva Extract on tert-butyl Hydroperoxide-induced Oxidative Hepatotoxicity", 환경생물, 27(2), pp.230~236 (2009), 한국환경생물학회
- Suh H, "Antioxidant activity of various solvent extracts from Allomyrina dichotoma(Arthropoda : Insecta)larvae", J. Photochem. Photobiol. B Biol, 99, pp.67~73 (2010)
- Niu L, "Novel skeleton compound Allomyrinanoid A and two purine alkaloids from the adult of Allomyrina dichotoma L", Bioorg. Med. Chem. Lett, 26, pp.366~369 (2016)
- Miyanoshita A, "Isolation and characterization of a new member of the insect defensin family from a beetle, Allomtrina dichotoma", Biochem. Biophy. Res. Commun, 220, pp.526~531 (1996)
- Sagisaka A, "Purification, characterization and gene expression of a glycine and proline-rich antibacterial protein family from larvae of a beetle, Allomtrina dichotoma", Insect Mol. Biol, 10, pp.293~302 (2001)
- Yamada M, "Effect of modified oligopeptides from the beetle Allomyrina dichotoma on Escherichia coli infection in mice", J. Vet. Med. Sci, 66, pp.137~142 (2004)
- Yamada M, "Therapeutic effect of modified oligopeptides from the beetle Allomyrina dichotoma on methicillin-resistant Staphylococcus aureus(MRSA)infection in mice", J. Vet. Med. Sci, 67, pp.1005~1011 (2005)
- Kumar P, "Antimicrobial peptides : diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo", Biomolecules, 8, pp.4~ (2018)
- Karima R, "The molecular pathogenesis of endotoxic shock and organ failure", Mol. Med. Today, 5, pp.123~132 (1999)
- Martin GS, "The epidemiology of sepsis in the United States from 1979through 2000", N. Engl. J. Med, 348, pp.1546~1554 (2003)
- Ren JD, "A synthetic cyclic peptide derived from Limulus anti-lipopolysaccharide factor neutralizes endotoxin in vitro and in vivo", Int. Immunopharmacol, 8, pp.775~781 (2008)
- Koyama Y, "Protective effects of antimicrobial peptides derived from the beetle Allomyrina dichotoma defensin on endotoxic shock in mice", Int. Immunopharmacol, 6, pp.232~240 (2006)
- Lehrer RI, "Designer assays for antimicrobial peptides", J. Immunol. Methods, 137, pp.167~173 (1991)
- Rosenfeld Y, "Lipopolysaccharide(Endotoxin)-host defense antibacterial peptides interactions : role in bacterial resistance and prevention of sepsis", Biochim. Biophys. Acta, 1758, pp.1513~1522 (2006)
- Bhor VM, "Polymyxin B : an ode to an old antidote for endotoxic shock", Mol. Biosyst, 1, pp.213~222 (2005)
- Brandenburg K, "Peptide-based treatment of sepsis", Appl. Microbiol. Biotechnol, 90, pp.799~808 (2011)
- Malmsten M, "Interactions of antimicrobial peptides with bacterial membranes and menbrane components", Curr. Top. Med. Chem, 16, pp.16~24 (2016)
- Lee E, "Insight into the antimicrobial activities of coprisin isolated from the dung beetle, Copris tripatitus, revealed by structureactivity relationships", Biochim. Biophys. Acta, 1828, pp.271~283 (2013)
- Nam HJ, "The insect peptide CopA3 inhibits lipopolysaccharideinduced macrophage activation", J. Pept. Sci, 18, pp.650~656 (2012)
- Qin H, "LPS induces CD40 gene expression through the activation of NF-kappaB and STAT-1α in macrophage and microglia", Blood, 106, pp.3114~3122 (2005)
- Scott MG, "Cutting edge : cationic antimicrobial peptides block the binding of lipopolysaccharide(LPS)to LPS binding protein", J. Immunol, 164, pp.549~553 (2000)
