МЕТАБОЛИЧЕСКАЯ АДАПТАЦИЯ ГЕЛЬМИНТОВ КИШЕЧНИКА РЫБ: ИНГИБИРУЮЩАЯ СПОСОБНОСТЬ ПО ОТНОШЕНИЮ К ПРОТЕАЗАМ У ЦЕСТОД TRIAENOPHORUS NODULOSUS
PDF

Ключевые слова

рыбы
цестоды
протеолитическая активность

Аннотация

Исследована ингибирующая способность по отношению к протеазам экстрактов плероцеркоидов из печени окуня (Perca fluviatilis Linnaeus), а также экскреторно-секреторных продуктов и экстрактов незрелых и зрелых цестод Triaenophorus nodulosus (Pallas, 1781), из кишечника щуки (Esox lucius Linnaeus). Установлено, что ингибирующей способностью по отношению к протеазам в различной степени обладают экскреторно-секреторные продукты и экстракты как незрелых, так и зрелых цестод T. nodulosus. Достоверное снижение активности отмечено при действии исследуемых образцов на активность коммерческого трипсина. Большей ингибирующей способностью по сравнению с экскреторно-секреторными продуктами обладают экстракты червей. При этом экстракт незрелых червей ингибирует активность протеаз сильнее, чем таковой зрелых. В большей степени ингибирующая способность связана с экстрактом червей, лишенных щеточной каймы, чем с фракцией щеточной каймы тегумента.

https://doi.org/10.31857/S0044452923050042
PDF

Литература

Scholz T, Kuchta R, Oros M (2021) Tapeworms as pathogens of fish: A review. Journal of Fish Diseases. 44:1883–1900. https://doi.org/10.1111/jfd.13526

Kuperman BI (1981) Tapeworms of the genus Trienophorus, parasites of fishes. New Delhi: Amerind Publishing Co. Pvt. Ltd.

Pappas PW, Narcisi EM, Rentko V (1983) Alteration in brush border membrane proteins and membrane-bound enzymes of the tapeworm Hymenolepis diminuta during development in the definitive host. Mol Bioch Parasitol 8:317–323.

Cwiklinski K, Dalton JP (2018) Advances in Fasciola hepatica research using ‘omics’ technologies. Int J Parasitol 48:321–331. https://doi.org/10.1016/j.ijpara.2017.12.001

Zhang Y, Guo J, He L, Zong H-Y, Cai G-B (2018) Isolation and characterization of a novel serine protease inhibitor, SjSPI, from Schistosoma japonicum. Parasitol Int 67:415–424. https://doi.org/10.1016/j.parint.2018.04.002

Zang X Maizels RM (2001) Serine proteinase inhibitors from nematodes and the arms race between host and pathogen. TRENDS Biochem Sci 26:191–197.

Morris SR, Sakanari JA (1994) Characterization of the serine protease and serine protease inhibitor from the tissue-penetrating nematode Anisakis simplex. J Biol Chem 269:27650–27656.

Kutyrev IA, Mazur OE, Goreva OB, Mordvinov VA (2020) A study of protein fractional composition during incubation of Diphyllobothrium dendriticum (Cestoda) plerocercoids in a medium containing blood serum of the host, the baikal omul Coregonus migratorius (Coregonidae). Biol Bull 47:490–496. https://doi.org/10.1134/S1062359020040081

Izvekova GI, Frolova TV, Izvekov EI (2017) Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda). Helminthologia 54:3–10. https://doi.org/10.1515/helm-2017-0001

Rogozhin E, Solovyev M, Frolova T, Izvekova G (2019) Isolation and partial structural characterization of new Kunitz-type trypsin inhibitors from the pike cestode Triaenophorus nodulosus. Mol Biochem Parasitol 233:111217. https://doi.org/10.1016/j.molbiopara.2019.111217

Oaks J, Knowles W, Cain G (1977) A simple method of obtaining an enriched fraction of tegumental brush border from Hymenolepis diminuta. J Parasitol 63:476–485.

Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochem 72:248–254.

Alarcón, FJ, Martínez TF, Barranco P, Cabello T, Díaz M, Moyano FJ (2002) Digestive proteases during development of larvae of red palm weevil, Rhynchophorus errugineus (Olivier, 1790) (Coleoptera: Curculionidae). Insect Biochem Mol Biol 32:265–274.

Nolasco-Soria H (2021) Improving and standardizing protocols for alkaline protease quantification in fish. Rev Aquacult 13:43–65. https://doi.org/10.1111/raq.12463

Holm H, Hanssen LE, Krogdahl A, Florholmen J (1988) High and low inhibitor soybean meals affect human duodenal proteinase activity differently: in vivo comparison with bovine serum albumin. J Nutrit 118:515–520.

Worthington Biochemical Corporation, 1991. Worthington Enzyme Manual: Enzymes, Enzyme Reagents. Freehold, N.J.

Zimic MJ, Infantes J, López C, Velásquez J, Farfán M, Pajuelo M, Sheen P, Verastegui M, Gonzalez A, García HH, Gilman RH (2007) Comparison of the peptidase activity in the oncosphere excretory/secretory products of Taenia solium and Taenia saginata. J Parasitol 93:727–734.

Пронина СВ, Пронин НМ (1988) Взаимоотношения в системах гельминты–рыбы. М.: Наука. [Pronina SV, Pronin NM (1988) Relationships in helminth–fish systems. M. Nauka (in Russ)]

Izvekova GI, Tyutin AV (2014) Activity of digestive enzymes and distribution of the trematode Bunodera luciopercae (Muller) in the intestine of juvenile perch infected with plerocercoids of Triaenophorus nodulosus (Pallas). Inland Water Biol 7:167–171. https://doi.org/10.1134/S1995082914010076

Frolova TF, Parshukov AN, Izvekova GI (2018) Activity of digestive enzymes in perch infected with Triaenophorus nodulosus (Pallas) plerocercoids. Inland Water Biol 11:501–506. https://doi.org/10.1134/S1995082918040053

Kochneva A, Drozdova P, Borvinskaya E (2020). The first transcriptomic resource for the flatworm Triaenophorus nodulosus (Cestoda: Bothriocephalidea), a common parasite of holarctic freshwater fish. Marine Genomics 51:100702. https://doi.org/10.1016/j.margen.2019.100702

Borvinskaya E, Kochneva A, Bedulina D, Sukhovskaya I, Smirnov L, Babkina I (2021) Comparative Analysis of Proteins of Functionally Different Body Parts of the Fish Parasites Triaenophorus nodulosus and Triaenophorus crassus. Acta Parasitol 66:1137–1150. https://doi.org/10.1007/s11686-021-00384-6

de Magalhaes MTQ, Mambelli FS, Santos BPO, Morais SB, Oliveira SC (2018) Serine protease inhibitors containing a Kunitz domain: their role in modulation of host inflammatory responses and parasite survival. Microb Infect 20:606–609. https://doi.org/10.1016/j.micinf.2018.01.003

Izvekova GI, Frolova TV, Izvekov EI, Kashinskaya EN, Solovyev MM (2021) Localization of the proteinase inhibitor activity in the fish cestode Eubothrium rugosum. J Fish Dis 44:1951–1958. https://doi.org/10.1111/jfd.13508

Kashinskaya EN, Simonov EP, Poddubnaya LG, Vlasenko PG, Shokurova AV, Parshukov AN, Andree KB, Solovyev MM (2023) Trophic diversification and parasitic invasion as ecological niche modulators for gut microbiota of whitefish. Front Microbiol 14:1090899. https://doi.org/10.3389/fmicb.2023.1090899

Lombardo JF, Pórfido JL, Sisti MS, Giorello AN, Rodríguez S, Córsico B,·Franchini GR (2022) Function of lipid binding proteins of parasitic helminths: still a long road. Parasitol Res 121:1117–1129. https://doi.org/10.1007/s00436-022-07463-1

Xu J, Wu L, Sun Y, Wei Y, Zheng L, Zhang J, Pang Z, Yang Y, Lu Y (2020) Proteomics and bioinformatics analysis of Fasciola hepatica somatic proteome in different growth phases. Parasitol Res 119:2837–2850. https://doi.org/10.1007/s00436-020-06833-x

Victor B, Kanobana K, Gabriël S, Polman K, Deckers N, Dorny P, Deelder AM, Palmblad M (2012) Proteomic analysis of Taenia solium metacestode excretion-secretion proteins. Proteomics 11:1860–1869.