Killing of Staphylococcus aureus by allylpyrocatechol is potentiated by induction of intracellular oxidative stress and inhibition of catalase activity

Journal of Integrative Medicine

Volumn 14, Issue 6, 2016, Pages 456-464

  Hussain, Roslinah Mohamad ^a   Abdullah, Noor Faradilla ^a   Amom, Zulkhairi ^a  

^a UNIVERSITI TEKNOLOGI MARA   (Malaysia)

Author keywords

alkyl hydroperoxide reductase; allylpyrocatechol; catalase; Piper betle; reactive oxygen species; Staphylococcus aureus; superoxide dismutase

Indexed keywords

ALLYLPYROCATECHOL; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; BETEL EXTRACT; CATALASE; DNA TOPOISOMERASE (ATP HYDROLYSING) A; HYDROGEN PEROXIDE; HYDROPEROXIDE REDUCTASE; OXYGEN; REACTIVE OXYGEN METABOLITE; RNA 16S; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CATECHOL DERIVATIVE; PLANT EXTRACT;

AHPC GENE; ANTIOXIDANT ACTIVITY; ARTICLE; BACTERIAL GENE; BACTERICIDAL ACTIVITY; CONTROLLED STUDY; DRUG EFFECT; DRUG MECHANISM; DRUG POTENCY; ENZYME ACTIVITY; ENZYME INHIBITION; GENE EXPRESSION; GENETIC TRANSCRIPTION; KATA GENE; LIVAK METHOD; MINIMUM INHIBITORY CONCENTRATION; NITROBLUE TETRAZOLIUM TEST; NONHUMAN; OXIDATIVE STRESS; PIPER BETLE; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; REAL TIME POLYMERASE CHAIN REACTION; SODA GENE; SODM GENE; STAPHYLOCOCCUS AUREUS; STATISTICAL MODEL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; HUMAN; METABOLISM; PIPER (PLANT);

ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CATALASE; CATECHOLS; HUMANS; HYDROGEN PEROXIDE; OXIDATIVE STRESS; PIPER; PLANT EXTRACTS; REACTIVE OXYGEN SPECIES; RNA, RIBOSOMAL, 16S; STAPHYLOCOCCUS AUREUS; SUPEROXIDE DISMUTASE;

EID: 85050579509     PISSN: 20954964     EISSN: None     Source Type: Journal    
DOI: 10.1016/S2095-4964(16)60279-0     Document Type: Article

References (40)

1. 1 Boucher, H, Miller, LG, Razonable, RR, Serious infections caused by methicillin-resistant Staphylococcus aureus. Clin Infect Dis 51:Suppl 2 (2010), S183–S197.
2. 2 Caksen, H, Oztürk, MK, Uzüm, K, Yüksel, S, Ustünbaş, HB, Pulmonary complications in patients with staphylococcal sepsis. Pediatr Int 42:3 (2000), 268–271.
3. 3 Gaupp, R, Ledala, N, Somerville, GA, Staphylococcal response to oxidative stress. Front Cell Infect Microbiol, 2, 2012, 33.
4. 4 Poole, K, Bacterial stress responses as determinants of antimicrobial resistance. J Antimicrob Chemother 67:9 (2012), 2069–2089.
5. 5 Horsburgh, MJ, Ingham, E, Foster, SJ, In Staphylococcus aureus fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J Bacteriol 183:2 (2001), 468–475.
6. 6 Nakonieczna, J, Michta, E, Rybicka, M, Grinholc, M, Gwizdek-Wiśniewska, A, Bielawski, KP, Superoxide dismutase is upregulated in Staphylococcus aureus following protoporphyrin-mediated photodynamic inactivation and does not directly influence the response to photodynamic treatment. BMC Microbiol, 10, 2010, 323.
7. 7 Clements, MO, Watson, SP, Foster, SJ, Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol 181:13 (1999), 3898–3903.
8. 8 Rocha, ER, Smith, CJ, Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis. J Bacteriol 181:18 (1999), 5701–5710.
9. 9 Chen, L, Xie, QW, Nathan, C, Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol Cell 1:6 (1998), 795–805.
10. 10 Cosgrove, K, Coutts, G, Jonsson, IM, Tarkowski, A, Kokai-Kun, JF, Mond, JJ, Foster, SJ, Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus. J Bacteriol 189:3 (2007), 1025–1035.
11. 11 Sharma, S, Khan, IA, Ali, I, Ali, F, Kumar, M, Kumar, A, Johri, RK, Abdullah, ST, Bani, S, Pandey, A, Suri, KA, Gupta, BD, Satti, NK, Dutt, P, Qazi, GN, Evaluation of the antimicrobial, antioxidant, and anti-inflammatory activities of hydroxychavicol for its potential use as an oral care agent. Antimicrob Agents Chemother 53:1 (2009), 216–222.
12. 12 Jesonbabu, J, Spandana, N, Lakshmi, AK, The potential activity of hydroxychavicol against pathogenic bacteria. J Bacteriol Parasitol 2:6 (2011), 2–5.
13. 13 Milton, PS, Muthumani, M, Shagirtha, K, Protective effect of Piper betle leaf extract against cadmium-induced oxidative stress and hepatic dysfunction in rats. Saudi J Biol Sci 19:2 (2012), 229–239.
14. 14 Mahfuzul, HM, Rattila, S, Asaduzzaman, SM, Bari, ML, Inatsu, Y, Kawamoto, S, Antibacterial activity of ethanol extract of betel leaf (Piper betle L.) against some food borne pathogens. Bangladesh J Microbiol 28:2 (2011), 58–63.
15. 15 Chakraborty, D, Shah, B, Antimicrobial, anti-oxidative and anti-hemolytic activity of Piper betle leaf extracts. Int J Pharm Pharm Sci 3:3 (2011), 192–199.
16. 16 Nalina, T, Rahim, ZHA, The crude aqueous extract of Piper betle L. and its antibacterial effect towards Streptococcus mutans. Am J Biotechnol Biochem 3 (2007), 10–15.
17. 17 Sarkar, D, Kundu, S, De, S, Hariharan, C, Saha, P, Manna, A, Chattopadhyay, S, Chatterjee, M, The antioxidant activity of allylpyrocatechol is mediated via decreased generation of free radicals along with escalation of antioxidant mechanisms. Phytother Res 27:3 (2013), 324–329.
18. 18 Ramji, N, Ramji, N, Iyer, R, Chandrasekaran, S, Phenolic antibacterials from Piper betle in the prevention of halitosis. J Ethnopharmacol 83:1–2 (2002), 149–152.
19. 19 Bhattacharya, S, Banerjee, D, Bauri, AK, Chattopadhyay, S, Bandyopadhyay, SK, Healing property of the Piper betle phenol, allylpyrocatechol against indomethacin-induced stomach ulceration and mechanism of action. World J Gastroenterol 13:27 (2007), 3705–3713.
20. 20 Sarkar, D, Saha, P, Gamre, S, Bhattacharjee, S, Hariharan, C, Ganguly, S, Sen, R, Mandal, G, Chattopadhyay, S, Majumdar, S, Chatterjee, M, Anti-inflammatory effect of allylpyrocatechol in LPS-induced macrophages is mediated by suppression of iNOS and COX-2 via the NF-κB pathway. Int Immunopharmacol 8:9 (2008), 1264–1271.
21. 21 Mula, S, Banerjee, D, Patro, BS, Bhattacharya, S, Barik, A, Bandyopadhyay, SK, Chattopadhyay, S, Inhibitory property of the Piper betle phenolics against photosensitization-induced biological damages. Bioorg Med Chem 16:6 (2008), 2932–2938.
22. 22 Becerra, MC, Albesa, I, Oxidative stress induced by ciprofloxacin in Staphylococcus aureus. Biochem Biophys Res Commun 297:4 (2002), 1003–1007.
23. 23 Livak, KJ, Schmittgen, TD, Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔct method. Methods 25:4 (2001), 402–408.
24. 24 Das, D, Saha, SS, Bishayi, B, Intracellular survival of Staphylococcus aureus: correlating production of catalase and superoxide dismutase with levels of inflammatory cytokines. Inflamm Res 57:7 (2008), 340–349.
25. 25 Das, D, Bishayi, B, Contribution of catalase and superoxide dismutase to the intracellular survival of clinical isolates of Staphylococcus aureus in murine macrophages. Indian J Microbiol 50:4 (2010), 375–384.
26. 26 Rintiswati, N, Wibawa, T, Asmara, W, Soebono, H, Effect of oxidative stress on AhpC activity and virulence in katG Ser315 Thr mycobacterium tuberculosis mutant. Indones J Biotechnol 16:2 (2011), 100–110.
27. 27 Helmann, JD, Wu, MF, Gaballa, A, Kobel, PA, Morshedi, MM, Fawcett, P, Paddon, C, The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors. J Bacteriol 185:1 (2003), 243–253.
28. 28 Abdullah, NF, Hussain, RM, Amom, Z, Effect of APC on killing of Staphylococcus aureus by oxidative stress agents. Jurnal Teknologi 78:5 (2016), 39–44.
29. 29 Newberry, KJ, Fuangthong, M, Panmanee, W, Mongkolsuk, S, Brennan, RG, Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR. Mol Cell 28:4 (2007), 652–664.
30. 30 Karavolos, MH, Horsburgh, MJ, Ingham, E, Foster, SJ, Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149:10 (2003), 2749–2758.
31. 31 Touati, D, Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions. J Bacteriol 170:6 (1988), 2511–2520.
32. 32 Procházková, D, Boušová, I, Wilhelmová, N, Antioxidant and prooxidant properties of flavonoids. Fitoterapia 82:4 (2011), 513–523.
33. 33 Rahal, A, Kumar, A, Singh, V, Yadav, B, Tiwari, R, Chakraborty, S, Dhama, K, Oxidative stress, prooxidants, and antioxidants: the interplay. Biomed Res Int, 2014, 2014, 761264.
34. 34 Valderas, MW, Hart, ME, Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus. J Bacteriol 183:11 (2001), 3399–3407.
35. 35 Rathee, JS, Patro, BS, Mula, S, Gamre, S, Chattopadhyay, S, Antioxidant activity of Piper betle leaf extract and its constituents. J Agric Food Chem 54:24 (2006), 9046–9054.
36. 36 Bhalerao, SA, Verma, DR, Gavankar, RV, Teli, NC, Yatin, YR, Didwana, VS, Trikannad, A, Phytochemistry, pharmacological profile and therapeutic uses of Piper betle Linn.—an overview. J Pharm Phytochem 1:2 (2013), 10–19.
37. 37 Hussain, RM, Din, NAM, Nasir, NNM, Piper betle ethanolic extract reduces neutrophil scavenging ability and possibly catalase activity in S. aureus. Int J Pharm Sci Rev Res 22:1 (2013), 35–40.
38. 38 Abrahim, NN, Kanthimathi, MS, Abdul-Aziz, A, Piper betle shows antioxidant activities, inhibits MCF-7 cell proliferation and increases activities of catalase and superoxide dismutase. BMC Complement Altern Med, 12(1), 2012, 220.
39. 39 Imlay, JA, Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77 (2008), 755–776.
40. 40 Seaver, LC, Imlay, JA, Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol 183:24 (2001), 7173–7181.