The effect of Triaenophorus nodulosus (Cestoda: Bothriocephalidea) infection on some biochemical parameters of the liver of Perca fluviatilis
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Natural infection of 2 to 6-year-old perch with the cestode parasites Triaenophorus nodulosus was shown to have minor effects on the studied components of the antioxidant defense system, nucleic acids degradation, and carbohydrate metabolism enzymes in the liver of the fish. The level of infection of 1–4 parasite larvae per fish observed in wild population of perch was shown to be moderate in terms of its effect on the health of the host fish. The activity of hepatic enzymes β-galactosidase, β-glucosidase, cathepsin D, and glutathione S-transferase showed different responses in infected males and females, which indicates different potential resistance of fish to the stress exposure between genders.
KeywordsHelminth Triaenophorus Cestoda Perca fluviatilis Invasion Biochemical status
The study was carried out under state order (Project No. 0218-2019-0075) and co-financed the Russian Foundation for Basic Research, Grant No. 17-04-01700 a. The research was carried out using the equipment of the Core Facility of the Karelian Research Centre of the Russian Academy of Sciences.
All authors have participated in conception and design, or analysis and interpretation of the data; drafting the article or revising it critically for important intellectual content; and approval of the final version.
Compliance with ethical standards
Conflict of interest
All authors declare that they have no conflict of interest.
All procedures followed were in accordance with the European Convention for the Protection of Vertebrate Animals used for Experimental and other Scientific Purposes (ETS No. 123) and the 8th Edition of the Guide for the Care and Use of Laboratory Animals (NRC 2011). All guidelines for use of animals were followed. This article does not contain any studies with human.
- Azizan S, Wan KL, Mohd-Adnan A (2014) Molecular characterisation and expression analysis of cathepsin D from the Asian seabass Lates calcarifer. Sains Malays 43:1139–1148Google Scholar
- Bergmeyer HU (1983) Methods of enzymatic analysis. Academic, New YorkGoogle Scholar
- Borvinskaya EV, Nemova NN, Smirnov LP (2011) Glutathione-S-transferase in fish of northern reservoirs: the effect of mineralization of the aquatic environment. Dokl Biochem Biophys 436:566–568 (in Russian) Google Scholar
- Boufana B, Zibrat U, Jehle R, Craig PS, Gassner H, Schabetsberger R (2011) Differential diagnosis of Triaenophorus crassus and T. nodulosus experimental infection in Cyclops abyssorum praealpinus (Copepoda) from the Alpine Lake Grundlsee (Austria) using PCR-RFLP. Parasitol Res 109:745–750. https://doi.org/10.1007/s00436-011-2317-4 CrossRefPubMedGoogle Scholar
- Cui SJ, Xu LL, Zhang T, Xu M, Yao J, Fang CY, Feng Z, Yang PY, Hu W, Liu F (2013) Proteomic characterization of larval and adult developmental stages in Echinococcus granulosus reveals novel insight into host–parasite interactions. J Proteomics 84:158–175. https://doi.org/10.1016/j.jprot.2013.04.013 CrossRefPubMedGoogle Scholar
- De la Torre-Escudero E, Valero L, Pérez-Sánchez R, Manzano-Román R, Oleaga A (2012) Proteomic identification of endothelial cell surface proteins isolated from the hepatic portal vein of mice infected with Schistosoma bovis. J Proteomics 77:129–143. https://doi.org/10.1016/j.jprot.2012.07.015 CrossRefPubMedGoogle Scholar
- Dezfuli BS, Giari L, Lorenzoni M, Manera M, Noga EJ (2014) Perch liver reaction to Triaenophorus nodulosus plerocercoids with an emphasis on piscidins 3,4 and proliferative cell nuclear antigen (PCNA) expression. Vet Parasitol 200:104–110. https://doi.org/10.1016/j.vetpar.2013.11.023 CrossRefPubMedGoogle Scholar
- Frank SN, Faust S, Kalbe M, Trubiroha A, Kloas W, Sures B (2011) Fish hepatic glutathione-S-transferase activity is affected by the cestode parasites Schistocephalus solidus and Ligula intestinalis: evidence from field and laboratory studies. Parasitology 138:939–944. https://doi.org/10.1017/S003118201100045X CrossRefPubMedGoogle Scholar
- Hassan AH, Al-Zanbagi NA, Al-Nabati EA (2015) Biochemical changes in muscles and liver in relation to helminth infection of Koshar fish, Epinephelus summana in Jeddah, Saudi Arabia. Am Eur J Agric Environ Sci 15:2064–2068. https://doi.org/10.5829/idosi.aejaes.2015.15.10.96223 CrossRefGoogle Scholar
- Hermes-Lima M (2004) Oxygen in biology and biochemistry: role of free radicals. In: Storey KB (ed) Functional metabolism: regulation and adaptation. Wiley, Hoboken, pp 319–368Google Scholar
- Ieshko EP (1988) Population biology of fish helminths. Science, Moscow (in Russian) Google Scholar
- Jiang WD, Liu Y, Hu K, Jiang J, Li SH, Feng L, Zhou XQ (2014) Copper exposure induces oxidative injury, disturbs the antioxidant system and changes the Nrf2/ARE (CuZnSOD) signaling in the fish brain: protective effects of myo-inositol. Aquat Toxicol 155:301–313. https://doi.org/10.1016/j.aquatox.2014.07.003 CrossRefPubMedGoogle Scholar
- Kuperman BI (1973) Tapeworms of the genus Triaenophorus—fish parasites. Science, Leningrad (in Russian) Google Scholar
- Levitsky AP, Barabash RD, Konovets VM (1973) Seasonal features of ribonuclease activity and α-amylase of saliva and salivary glands in Wistar rats. In: Kreps EM (ed) Biochemical evolution. Science, Leningrad, pp 192–195 (in Russian)Google Scholar
- Liu F, Lu J, Hu W, Wang SY, Cui SJ, Chi M, Yan Q, Wang XR, Song HD, Xu XN, Wang JJ, Zhang XL, Zhang X, Wang ZQ, Xue CL, Brindley PJ, McManus DP, Yang PY, Feng Z, Chen Z, Han ZG (2006) New perspectives on host–parasite interplay by comparative transcriptomic and proteomic analyses of Schistosoma japonicum. PLoS Pathog 2:e29. https://doi.org/10.1371/journal.ppat.0020029 CrossRefPubMedPubMedCentralGoogle Scholar
- Lowry OH, Rosebrough NJ, Fall AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275Google Scholar
- Lysenko LA, Nemova NN, Kantserova NP (2011) Proteolytic regulation of biological processes. KarRC RAS, Petrozavodsk (in Russian) Google Scholar
- Nemova NN, Bondareva LA (2005) Proteolytic enzymes. KarRC RAS, Petrozavodsk (in Russian) Google Scholar
- Pokrovsky AA, Kravchenko LV, Tutel’jan VA (1971) Study of the activity of lysosome enzymes under the action of aflatoxin and mitomycin C. Biochemistry (Moscow) 36:690–696 (in Russian) Google Scholar
- Pronina SV, Pronin NM (1988) Relationships in worm–fish systems (tissue, organ, and whole body levels). Nauka, Moscow (in Russian) Google Scholar
- Robinson MW, Menon R, Donnelly SM, Dalton JP, Ranganathan S (2009) An integrated transcriptomics and proteomics analysis of the secretome of the helminth pathogen Fasciola hepatica: proteins associated with invasion and infection of the mammalian host. Mol Cell Proteomics 8:1891–1907. https://doi.org/10.1074/mcp.M900045-MCP200 CrossRefPubMedPubMedCentralGoogle Scholar
- Shishova-Kasatochkina OA, Leutskaya ZK (1979) Biochemical aspects of the relationship between helminth and host (exchange of proteins, vitamins and steroids in the process of parasitism). Science, Moscow (in Russian) Google Scholar
- Sidorov VS, Vysotskaya RW, Smirnov LP, Guryanova SD (1989) Comparative biochemistry of fish helminths. Amino acids, proteins, lipids. Nauka, Leningrad (in Russian) Google Scholar
- Skálová L, Krízová V, Cvilink V, Szotáková B, Storkánová L, Velík J, Lamka J (2007) Mouflon (Ovismusimon) dicrocoeliosis: effects of parasitosis on the activities of biotransformation enzymes and albendazole metabolism in liver. Vet Parasitol 31:254–262. https://doi.org/10.1016/j.vetpar.2007.02.026 CrossRefGoogle Scholar
- Sukhovskaya IV, Borvinskaya EV, Smirnov LP, Nemova NN (2010) Comparative analysis of methods for determination of protein concentration-spectrophotometry in the range 200–220 nm and according to Bradford. Trans KarRC RAS 2:68–71Google Scholar
- Vysotskaya RU, Nemova NN (2008) Lysosomes and lysosomal enzymes of fish. Science, Moscow (in Russian) Google Scholar
- Vysotskaya RU, Ieshko EP, Evseeva NV (2003) A comparative biochemical research in the Schistocephalus solidus (Cestoda)—three-spined stickleback Gasterosteus aculeatus L. system. Parazitologia 37:503–511 (in Russian) Google Scholar