Evaluation of catalase activity of clinical and environmental isolates of Aspergillus species
Abstract
Background and Objectives: Catalases are a good scavenger of H2O2 which degrades hydrogen peroxide into water and oxygen. They are considered as a virulence factor that are present in both spores and hypha of fungi. There is limited data regarding catalase activity in Aspergillus species. This study aimed to assess the mycelial catalase activity of clinical and environmental isolates of Aspergillus niger, A. tubingensis, A. flavus, A. luchuensis, A. piperis and A. terreus.
Materials and Methods: Briefly, clinical and environmental Aspergillus species were used in the current study. Catalase activity was assessed for both groups of isolates including 13 A. flavus (12 clinical, 1 environmental), 13 A. terreus (8 clinical, 5 environmental), 26 A. tubingensis (13 clinical, 13 environmental), and 44 A. niger (25 environmental, 19 clinical) species. Fungal balls of mycelia were separated from the liquid culture and were crushed using homogenizer. The supernatants were collected and used for a catalase activity assay.
Results: Totally, in our study 98 Aspergillus including 45 environmental and 53 clinical isolates were assessed for catalase activity. High catalase activity was detected among environmental Aspergillus species (Mean= 1.62 mU/ml) and the mean of mycelial catalase activity among clinical A. terreus isolates was higher than environmental strains.
Conclusion: In summary, mycelial catalase activity varied among species and environmental isolates demonstrated higher catalase activity. Totally a significant difference was found between clinical and environmental Aspergillus isolates.
2. Grigoras AG. Catalase immobilization - A review. Biochem Eng J 2017;117:1-20.
3. Day BJ. Catalytic antioxidants: a radical approach to new therapeutics. Drug Discov Today 2004;9:557-566.
4. Urban CF, Nett JE. Neutrophil extracellular traps in fungal infection. Semin Cell Dev Biol 2019;89:47-57.
5. Warris A, Ballou ER. Oxidative responses and fungal infection biology. Semin Cell Dev Biol 2019;89:34-46.
6. Petrova VY, Rasheva TV, Kujumdzieva AV. Catalase enzyme in mitochondria of Saccharomyces cerevisiae. Electron J Biotechnol 2002;5:11-12.
7. Skoneczny M, Rytka J. Oxygen and haem regulate the synthesis of peroxisomal proteins: catalase A, acyl-CoA oxidase and Pex1p in the yeast Saccharomyces cerevisiae; the regulation of these proteins by oxygen is not mediated by haem. Biochem J 2000;350:313-319.
8. Linares CE, Giacomelli SR, Altenhofen D, Alves SH, Morsch VM, Schetinger MR. Fluconazole and amphotericin-B resistance are associated with increased catalase and superoxide dismutase activity in Candida albicans and Candida dubliniensis. Rev Soc Bras Med Trop 2013;46:752-758.
9. Giles SS, Stajich JE, Nichols C, Gerrald QD, Alspaugh JA, Dietrich F, et al. The Cryptococcus neoformans catalase gene family and its role in antioxidant defense. Eukaryot Cell 2006;5:1447-1459.
10. Calera JA, Sanchez-Weatherby J, Lopez-Medrano R, Leal F. Distinctive properties of the catalase B of Aspergillus nidulans. FEBS Lett 2000;475:117-120.
11. Scherer M, Wei H, Liese R, Fischer R. Aspergillus nidulans catalase-peroxidase gene (cpeA) is transcriptionally induced during sexual development through the transcription factor StuA. Eukaryot Cell 2002;1:725-735.
12. Nekiunaite L, Arntzen MØ, Svensson B, Vaaje-Kolstad G, Abou Hachem M. Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches. Biotechnol Biofuels 2016;9:187.
13. Rouein S, Ghasemi F, Badiee P. Compare catalase activity between Aspergillus flavus and A. fumigatus, isolated from clinical and environmental specimens. Jundishapur J Microbiol 2020;13(8):e103634.
14. Boysen JM, Saeed N, Wolf T, Panagiotou G, Hillmann F. The peroxiredoxin Asp f3 acts as redox sensor in Aspergillus fumigatus. Genes (Basel) 2021;12:668.
15. Goetz KE, Coyle CM, Cheng JZ, O’Connor SE, Panaccione DG. Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I in Aspergillus fumigatus. Curr Genet 2011;57:201-211.
16. Hivary S, Fatahinia M, Halvaeezadeh M, Zarei Mahmoudabadi A. The potency of luliconazole against clinical and environmental Aspergillus nigri complex. Iran J Microbiol 2019;11:510-519.
17. Moslem M, Zarei Mahmoudabadi A. The high efficacy of luliconazole against environmental and otomycosis Aspergillus flavus strains. Iran J Microbiol 2020;12:170-176.
18. Wang ZL, Zhang LB, Ying SH, Feng MG. Catalases play differentiated roles in the adaptation of a fungal entomopathogen to environmental stresses. Environ Microbiol 2013;15:409-418.
19. Shibuya K, Paris S, Ando T, Nakayama H, Hatori T, Latge JP. Catalases of Aspergillus fumigatus and inflammation in aspergillosis. Nihon Ishinkin Gakkai Zasshi 2006;47:249-255.
20. Paris S, Wysong D, Debeaupuis JP, Shibuya K, Philippe B, Diamond RD, et al. Catalases of Aspergillus fumigatus. Infect Immun 2003;71:3551-3562.
21. Gallin JI, Alling DW, Malech HL, Wesley R, Koziol D, Marciano B, et al. Itraconazole to prevent fungal infections in chronic granulomatous disease. N Engl J Med 2003;348:2416-2422.
22. Yun Y, Lu Z, Yang J, Liang T, Xiao G, Qiao Y, et al. Electrochemical analysis of specific catalase activity during development of Aspergillus flavus and its correlation with aflatoxin B1 production. Food Chem 2021;337:127978.
23. Zhu Z, Yang M, Bai Y, Ge F, Wang S. Antioxidant-related catalase CTA1 regulates development, aflatoxin biosynthesis, and virulence in pathogenic fungus Aspergillus flavus. Environ Microbiol 2020;22:2792-2810.
24. Romsdahl J, Blachowicz A, Chiang AJ, Singh N, Stajich JE, Kalkum M, et al. Characterization of Aspergillus niger isolated from the international space station. mSystems 2018;3(5):e00112-18.
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Issue | Vol 14 No 1 (2022) | |
Section | Original Article(s) | |
DOI | https://doi.org/10.18502/ijm.v14i1.8815 | |
Keywords | ||
Catalase; Aspergillus; Virulence factor; Clinical; Aspergillosis |
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