Oxidative Damage and Antioxidant Response of Acinetobacter calcoaceticus, Pseudomonas putida and Rhodococcus erythropolis Bacteria during Antibiotic Treatment

Capa

Citar

Texto integral

Acesso aberto Acesso aberto
Acesso é fechado Acesso está concedido
Acesso é fechado Acesso é pago ou somente para assinantes

Resumo

In this work, oxidative damage and the level of antioxidant response in Acinetobacter calcoaceticus, Pseudomonas putida, and Rhodococcus erythropolis cells under the influence of such antibiotics as ampicillin, azithromycin, rifampicin, tetracycline, and ceftriaxone were studied. The level of protein carboxylation and lipid peroxidation (LPO), as well as the activity of superoxide dismutase (SOD), catalase, glutathione reductase (GR), and the level of glutathione 3 and 6 hours after antibiotic treatment of bacteria were assessed. It is observed that SOD induction occurs earlier and is more active than catalase induction. In A. calcoaceticus, SOD is induced together with protein carboxylation and probably protects them from oxidative damage, while catalase induction correlates with LPO. A positive correlation is also noted between catalase activity and glutathione content in R. erythropolis. Catalase activity increases insignificantly and even decreases under the studied antibiotics influence, which is associated with an insignificant level of lipid peroxidation in most prokaryotes. On the other hand, low catalase activity can contribute to genome destabilization as a result of oxidative stress and enhance the adaptive evolution of bacteria.

Texto integral

Acesso é fechado

Sobre autores

I. Sazykin

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

A. Plotnikov

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

O. Lanovaya

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

K. Onasenko

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

A. Polinichenko

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

A. Mezga

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

T. Azhogina

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

A. Litsevich

Southern Federal University

Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

M. Sazykina

Southern Federal University

Autor responsável pela correspondência
Email: samara@sfedu.ru
Rússia, Rostov-on-Don, 344090

Bibliografia

  1. Yoneyama H., Katsumata R. // Biosci. Biotechnol. Biochem. 2006. V. 70. № 5. P. 1060–1075.
  2. Фурман Ю.В., Артюшкова Е. Б., Аниканов А. В. // Актуальные проблемы социально-гуманитарного и научно-технического знания. 2019. № 1. С. 1–3.
  3. Пескин А.В. // Биохимия. 1997. Т. 62. № 12. С. 1571–1578.
  4. Imlay J.A. // Cur. Opin. Microbiol. 2015. V. 24. P. 124–131.
  5. Sazykin I.S., Sazykina M. A. // Gene. 2023. V. 857. P. 147170. https://doi.org/10.1016/j.gene.2023.147170
  6. Goyal A. // iScience. 2022. V. 25. № 5. P. 104312.
  7. Levine R.L., Garland D., Oliver C. N., Amici A., Climent I., Lenz A. G. et al. // Methods Enzymol. 1990. V. 186. P. 464–478.
  8. Дубинина Е.Е., Бурмистров С. О., Ходов Д. А., Поротов Г. Е. // Вопросы медицинской химии. 1995. Т. 41. № 1. С. 24–26.
  9. Стальная И.Д., Гаришвили Т. Г. // Современные методы в биохимии. 1977. Т. 2. № 3. С. 66–68.
  10. Королюк М. А., Иванова Л. К., Майорова И. Г., Токарева В. А. //Лабораторное дело. 1988. № 4. С. 44–47.
  11. Сирота Т.В. // Вопросы медицинской химии. 1999. Т. 45. № 3. С. 263–272.
  12. Ellman G.L. // Arch. Biochem. Biophys. 1959. V. 82. № 1. P. 70–77.
  13. Юсупова Л.Б. // Лабораторное дело. 1989. Т. 4. № 19–21. С. 13.
  14. Wanarska E., Mielko K. A., Maliszewska I., Młynarz P. // Sci. Rep. 2022. V. 12. № 1. P. 1913.
  15. Shin B., Park C., Park W. //Appl. Microbiol. Biotechnol. 2020. Т. 104. С. 1423–1435.
  16. Belenky P., Ye J. D., Porter C. B., Cohen N. R., Lobritz M. A., Ferrante T. et al. // Cell Rep. 2015. V. 13. № 5. P. 968–980.
  17. Brogden R.N., Ward A. // Drugs. 1988. V. 35. № 6. P. 604–645.
  18. Постникова Л.Б., Соодаева С. К., Климанов И. А., Кубышева Н. И., Афиногенов К. И., Глухова М. В., Никитина Л. Ю. // Пульмонология. 2017. V. 27. № 5. P. 664–671.
  19. Куликова Н. А. // Международный студенческий научный вестник. 2017. № 4–5. С. 614–615.
  20. Weimer A., Kohlstedt M., Volke D. C., Nikel P. I., Wittmann C. // Appl. Microbiol. Biotechnol. 2020. V. 104. P. 7745–7766.S
  21. Nikel P. I., Fuhrer T., Chavarría M., Sánchez-Pascuala A., Sauer U., de Lorenzo V. // ISME J. 2021. V. 15. № 6. P. 1751–1766.
  22. Van Acker H., Gielis J., Acke M., Cools F., Cos P., Coenye T. // PloS One. 2016. V. 11. № 7. e0159837. https://doi.org/10.1371/journal.pone.0159837
  23. Pátek M., Grulich M., Nešvera J. // Biotechnol. Adv. 2021. V. 53. P. 107698.
  24. Urbano S. B., Di Capua C., Cortez N., Farías M. E., Alvarez H. M. // Extremophiles. 2014. V. 18. P. 375–384.
  25. Meireles A., Faia S., Giaouris E., Simões M. // Biofouling. 2018. V. 34. № 10. P. 1150–1160.
  26. Ren X., Zou L., Holmgren A. // Curr. Med. Chem. 2020. V. 27. № 12. P. 1922–1939. https://doi.org/10.2174/0929867326666191007163654
  27. Cleeland R., Squires E. // Am. J. Med. 1984. V. 77. (4C). P. 3–11.
  28. Mourenza Á., Gil J. A., Mateos L. M., Letek M. // Antioxidants. 2020. V. 9. № 5. P. 361.
  29. Aguilera J., Rautenberger R. // Oxidative Stress in Aquatic Ecosystems. 2011. P. 58–71. https://doi.org/10.1002/9781444345988.ch4
  30. Martins D., McKay G., Sampathkumar G., Khakimova M., English A. M., Nguyen D. // PNAS. 2018. V. 115. № 39. P. 9797–9802.
  31. Heindorf M., Kadari M., Heider C., Skiebe E., Wilharm G. // PloS One. 2014. V. 9. № 7. P. e101033.
  32. Retsema J., Girard A., Schelkly W., Manousos M., Anderson M., Bright G. et al. // Antimicrob. Agents Сhemother. 1987. V. 31. № 12. P. 1939–1947.
  33. Mirzaei R., Mesdaghinia A., Hoseini S. S., Yunesian M. // Chemosphere. 2019. V. 221. P. 55–66.
  34. Ramanathan S., Arunachalam K., Chandran S., Selvaraj R., Shunmugiah K. P., Arumugam V. R. // J. Аppl. Microbiol. 2018. V. 125. № 1. P. 56–71. https://doi.org/10.1111/jam.13741.
  35. Zhang Y.N., Duan K. M. // Sci. China C Life Sci. 2009. V. 52. № 6. P. 501–505.
  36. Daschner F.D., Frank U. // Infection. 1989. V. 17. № 4. P. 272–274.
  37. Gnann Jr J. W., Goetter W. E., Elliott A. M., Cobbs C. G. // Antimicrob. Agents Chemother // 1982. V. 22. № 1. P. 1–9.
  38. El-Barbary M.I., Hal A. M. // J. Aquac. Res. Development. 2017. V. 8. № 7. P. 1–7. https://doi.org/10.4172/2155-9546.1000499
  39. Konikkat S., Scribner M. R., Eutsey R., Hiller N. L., Cooper V. S., McManus J. // PLoS genetics. 2021. V. 17. № 7: e1009634. https://doi.org/10.1371/journal.pgen.1009634
  40. Elbehiry A., Marzouk E., Aldubaib M., Moussa I., Abalkhail A., Ibrahem M. et al. // AMB Express. 2022. V. 12. № 1. P. 53. https://doi.org/10.1186/s13568-022-01390-1
  41. Plaggenborg R., Overhage J., Loos A., Archer J. A. C., Lessard P., Sinskey A. J. et al. // Appl. Microbiol. Biotechnol. 2006. V. 72. № 4. P. 745–755.
  42. Stancu M. M. // J. Environ. Sci. (Shina) 2014. V. 26. № 10. P. 2065–2075. https://doi.org/10.1016/j.jes.2014.08.006
  43. Yamshchikov A.V., Schuetz A., Lyon G. M. // Lancet Infecti. Dis. 2010. V. 10. № 5. P. 350–359.
  44. McNeil M.M., Brown J. M. // Eur. J. Epidemiol. 1992. V. 8. № 3. P. 437–443.
  45. Asoh N., Watanabe H., Fines-Guyon M., Watanabe K., Oishi K., Kositsakulchai W. et al. // J. Clin. Microbiol. 2003. V. 41. № 6. P. 2337–2340.
  46. Vaubourgeix J., Lin G., Dhar N., Chenouard N., Jiang X., Botella H. et al. // Cell Host & Microbe. 2015. V. 17. № 2. P. 178–190.
  47. Nyström T. // EMBO J. 2005. V. 24. № 7. P. 1311–1317.

Arquivos suplementares

Arquivos suplementares
Ação
1. JATS XML
Baixar
2. Fig. 1. The content of carbonyl groups (nM phenylhydrazones/mg protein) in the proteins of the studied bacterial strains after treatment with antibiotics: 1 - control; 2 - azithromycin; 3 - ampicillin; 4 - rifampicin; 5 - tetracycline; 6 - ceftriaxone; a - 3 h, b - 6 h. * The differences are statistically significant at p < 0.05.

Baixar (179KB)
Metadados
3. Fig. 2. Lipid peroxidation (MDA, nM/ml) in the studied bacterial strains after treatment with antibiotics: 1 - control; 2 - azithromycin; 3 - ampicillin; 4 - rifampicin; 5 - tetracycline; 6 - ceftriaxone; a - 3 h, b - 6 h. * The differences are statistically significant at p < 0.05.

Baixar (178KB)
Metadados
4. Fig. 3. SOD activity (U/mg protein × min) under the influence of antibiotics on the studied bacterial strains: 1 — control; 2 — azithromycin; 3 — ampicillin; 4 — rifampicin; 5 — tetracycline; 6 — ceftriaxone; a — 3 h, b — 6 h. * Differences are statistically significant at p < 0.05.

Baixar (149KB)
Metadados
5. Fig. 4. Catalase activity (nM H2O2/mg protein) under the influence of antibiotics on the studied bacterial strains: 1 — control; 2 — azithromycin; 3 — ampicillin; 4 — rifampicin; 5 — tetracycline; 6 — ceftriaxone; a — 3 h, b — 6 h. * Differences are statistically significant at p < 0.05.

Baixar (184KB)
Metadados
6. Fig. 5. Glutathione concentration (μM GSH/g protein) upon exposure to antibiotics on the studied bacterial strains: 1 — control; 2 — azithromycin; 3 — ampicillin; 4 — rifampicin; 5 — tetracycline; 6 — ceftriaxone; a — 3 h, b — 6 h. * Differences are statistically significant at p < 0.05.

Baixar (143KB)
Metadados
7. Fig. 6. Glutathione reductase activity (IU GR/g protein) upon exposure to antibiotics on the studied bacterial strains: 1 — control, without antibiotic; 2 — azithromycin; 3 — ampicillin; 4 — rifampicin; 5 — tetracycline; 6 — ceftriaxone; a — 3 h, b — 6 h. * Differences are statistically significant at p < 0.05.

Baixar (186KB)
Metadados
8. Fig. 7. Correlation between the activity of antioxidant enzymes and oxidative damage to bacterial cell components in the studied strains (significant values ​​are highlighted in color, p < 0.05). A — SOD, B — catalase, C — GSH, D — GR, D — protein carboxylation, E — LPO.

Baixar (111KB)
Metadados

Declaração de direitos autorais © Russian Academy of Sciences, 2024