Antiproliferative Activity of Crude Marcescin on Human Laryngx Epidermoid Carcinoma (Hep-2) Cell Line in Vitro Study

Riad M. Abdulredha; Hind Hussein Obaid

doi:10.30526/38.3.3742

Authors

Riad M. Abdulredha Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq. https://orcid.org/0009-0007-7966-8458
Hind Hussein Obaid Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq. https://orcid.org/0000-0002-2046-7834

DOI:

https://doi.org/10.30526/38.3.3742

Keywords:

Serratia marcescens, Marcescin, Cytotoxicity, Hep-2 cell line, Inhibition rate

Abstract

Marcescin is a bacteriocin that is extracted from isolates of Serratia marcescens, which is a gram-negative bacterium that belongs to the family Enterobacteraeaceae and is considered a nosocomial pathogenic bacteria. In this research, the toxic effect of crude marcescin extracted from the S. marcescens bacteria on the human laryngx epidermoid carcinoma (Hep-2) cell line was investigated. S. marcescens was isolated from blood, urine, and stool samples of patients from Nursing House Hospital, Baghdad Teaching Hospital, and Teaching Laboratories of Medical City by using a series of dilutions to concentrations of (0.00, 1.95, 3.9, 7.8, 15.62, 31.25, 62.5, 125, 250, 500, and 1000) µg/ml and an exposure time of (24, 48, and 72) hours. The results showed significant differences (P≤0.05) in the IR values (100–2%) at the concentrations (1000–1.95) µg/ml when compared with the control (100%); there were also significant differences after 48 and 72 hours. The results showed that high concentrations caused a high rate of inhibition at concentrations (1000, 500, and 250) µg/m where the rate of inhibition was (100, 67, and 58) after 24 hours, then the rate of inhibition began to decrease gradually, reaching 2% at the lowest concentration of 1.95. It is clear that Hep-2 cells are sensitive to marcescin, and their sensitivity increases exponentially with increasing concentration and time of exposure

Author Biographies

Riad M. Abdulredha, Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq.

Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq.
Hind Hussein Obaid, Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq.

Department of Biology, College of Science, University of Baghdad, Baghdad, Iraq.

References

1. Baindara P, Mandal SM. Bacteria and bacterial anticancer agents as a promising alternative for cancer therapeutics. Biochimie 2020;177:164–189. https://doi.org/10.1016/j.biochi.2020.07.020

2. Kaur B, Kumar S, Kaushik BK. Recent advancements in optical biosensors for cancer detection. Biosens Bioelectron 2022;197:113805. https://doi.org/10.1016/j.bios.2021.113805

3. Hassanpour SH, Dehghani M. Review of cancer from perspective of molecular. J Cancer Res Pract 2017;4(4):127–129. https://doi.org/10.1016/j.jcrpr.2017.07.001

4. Mahdi RH, Hasan SA, Hasan JM. The effect of Serratia marcescens protease on human lymphocytes transformation. Iraqi J Sci 2013;54(3):531–535. 531-535. https://ijs.uobaghdad.edu.iq/index.php/eijs/article/view/12113.

5. Dicks LM, Vermeulen W. Do bacteria provide an alternative to cancer treatment and what role does lactic acid bacteria play? Microorganisms 2022;10(9):1733. https://doi.org/10.3390/microorganisms10091733.

6. Coley WB. The treatment of inoperable sarcoma by bacterial toxins (the mixed toxins of the Streptococcus erysipelas and the Bacillus prodigiosus). Proc R Soc Med 1910;3(Surg Sect):1–48.

7. Wiemann B, Starnes CO. Coley’s toxins, tumor necrosis factor and cancer research: a historical perspective. Pharmacol Ther 1994;64(3):529–564. https://doi.org/10.1016/0163-7258(94)90023-x.

8. Molujin AM, Abbasiliasi S, Nurdin A, Lee PC, Gansau JA, Jawan R. Bacteriocins as potential therapeutic approaches in the treatment of various cancers: a review of in vitro studies. Cancers 2022;14(19):4758. https://doi.org/10.3390/cancers14194758.

9. Kaur S, Kaur S. Bacteriocins as potential anticancer agents. Front Pharmacol 2015;6:272. https://doi.org/10.3389/fphar.2015.00272.

10. Hussein AR, Khalaf ZZ, Samir Z, Samir R. The antibacterial activity of crude bacteriocin-like substance against food borne bacterial pathogens. Iraqi J Sci 2018; 59(1A): 16-24. https://ijs.uobaghdad.edu.iq/index.php/eijs/article/view/152.

11. Salman SM, Obaid HH. Assessment resistance of gram negative gut microbiota for antibiotics. Bioinfolet 2023;20(2a):147–152.

12. Al-Saeedi BSM, Luti KJK. Bacteriocin from Streptococcus salivarius optimized statistically by response surface methodology active against different clinical oral pathogenic Streptococci. Iraqi J Sci 2018;59(1C): 463-475. https://ijs.uobaghdad.edu.iq/index.php/eijs/article/view/271.

13. Traub WH, Raymond EA, Startsman TS. Bacteriocin (marcescin) typing of clinical isolates of Serratia marcescens. Appl Microbiol 1971;21(5):837–840. https://doi.org/10.1128/am.21.5.837-840.1971.

14. Šmajs D, Weinstock GM. The iron and temperature regulated cjrBC genes of Shigella and enteroinvasive Escherichia coli strains code for colicin Js uptake. J Bacteriol 2001;183(13):3958–3966. https://doi.org/10.1128/jb.183.13.3958-3966.2001.

15. Baindara P, Korpole S, Grover V. Bacteriocins: perspective for the development of novel anticancer drugs. Appl Microbiol Biotechnol 2018;102:10393–10408. https://doi.org/10.1007/s00253-018-9420-8.

16. Al Madboly LA, El Deeb NM, Kabbash A, Nael MA, Kenawy AM, Ragab AE. Purification, characterization, identification, and anticancer activity of a circular bacteriocin from Enterococcus thailandicus. Front Bioeng Biotechnol 2020;8:450. https://doi.org/10.3389/fbioe.2020.00450.

17. Herschman HR, Helinski DR. Purification and characterization of colicin E2 and colicin E3. J Biol Chem 1967;242(22):5360–5368. https://doi.org/10.1016/S0021-9258(18)99436-6.

18. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 1976;72(1–2):248–254. https://doi.org/10.1016/0003-2697(76)90527-3.

19. Šmajs D, Pilsl H, Braun V. Colicin U, a novel colicin produced by Shigella boydii. J Bacteriol 1997;179(15):4919–4928. https://doi.org/10.1128/jb.179.15.4919-4928.1997.

20. Freshney RI. Culture of Animal Cells: a Manual for Basic Technique. 4th ed. New York: Wiley-Liss; 2000.

21. Betancur Galvis LA, Saez J, Granados H, Salazar A, Ossa JE. Antitumor and antiviral activity of Colombian medicinal plant extracts. Mem Inst Oswaldo Cruz 1999;94:531–535. https://doi.org/10.1590/S0074-02761999000400011.

22. Betancur Galvis LA, Morales GE, Forero JE, Roldan J. Cytotoxic and antiviral activities of Colombian medicinal plant extracts of the Euphorbia genus. Mem Inst Oswaldo Cruz 2002;97:541–546. https://doi.org/10.1590/S0074-02762002000400024.

23. Gao S, Yu BP, Li Y, Dong WG, Luo HS. Antiproliferative effect of octreotide on gastric cancer cells mediated by inhibition of Akt/PKB and telomerase. World J Gastroenterol 2003;9(10):2362–2364. https://doi.org/10.3748/wjg.v9.i10.2362.

24. Al Qassab AO, Al Khafaji ZM. Effect of different conditions on inhibition activity of enteric lactobacilli against diarrhea-causing enteric bacteria. J Agric Sci 1992;3(1):18–26.

25. Fumarola D, Bello P, Palma R, Miragliotta G, Panaro A. Bacteriocins as cytotoxic agents in experimental neoplasms: considerations on the role of possible contaminants. Giorn Bact Virol Immunol 1977;70(1–6):87–93.

26. Saito H, Watanabe T. Effect of a bacteriocin produced by Mycobacterium smegmatis on growth of cultured tumor and normal cells. Cancer Res 1979;39(12):5114–5117.

27. Farkas Himsley H, Yu H. Purified colicin as cytotoxic agent of neoplasia: comparative study with crude colicin. Cytobios 1985;42(167–168):193–207.

28. Obaid HH, Essa RH, Yaseen NY. Cytotoxicity of non-bound colicins extracted from Escherichia coli on normal white blood cells and myeloblast isolated from acute myeloid leukemia blood patients. Iraqi J Sci 2010;51(4):528–538. https://doi.org/10.24996/ijs.2010.51.4.%g.

29. Obaid HH, Essa RH, Yaseen NY. Cytotoxicity of non-bound colicins extracted from Escherichia coli on human larynx epidermoid carcinoma (Hep 2) cell line. Third National Feminist Scientific Conference, Ministry of Science and Technology; 2019.

30. Farkas Himsley H, Cheung R. Bacterial proteinaceous products (bacteriocins) as cytotoxic agents of neoplasia. Cancer Res 1976;36(10):3561–3567.

31. Farkas Himsley H. Sensitivity of various malignant cell lines to partially purified bacteriocins: inherent and proliferative dependence. Microbios Lett 1988;39(154):57–66. https://doi.org/10.1007/978-3-642-76974-0_47

32. Nes IF, Brede DA, Holo H. The non-lantibiotic heat stable bacteriocins in gram positive bacteria. In: Kastin, editor. Handbook Biol Active Peptid. Academic Press; 2006. p. 107–114. https://doi.org/10.1016/B978-012369442-3/50020-9

33. Viejo MB, Gargallo D, Ferrer S, Enfedaque J, Regué M. Cloning and DNA sequence analysis of a bacteriocin gene of Serratia marcescens. Microbiology 1992;138(8):1737–1743.

34. Farkas Himsley H, Zhang YS, Yuan M, Musclow CE. Partially purified bacteriocin kills malignant cells by apoptosis: programmed cell death. Cell Mol Biol (Noisy le Grand) 1992;38(5–6):643–651. https://doi.org/10.1099/00221287-138-8-1737.

35. Mittelman M, Farkas Himsley H, Haran Ghera N. Recognition of T cell murine leukemia by bacteriocin (colicin); correlation with transplantation experiments. Leuk Res 1987;11(3):215–222. https://doi.org/10.1016/0145-2126(87)90045-2