Protein Profile of the Incubation Medium and Cestode Extract from the Intestines of Various Fish Species

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

The protein composition of the incubation medium and extracts of various types of cestodes inhabiting the intestines of freshwater fish was investigated. Proteins with apparent molecular weights from 10 to 312.5 kDa were found in both biological media of worms. In most of the investigated worms, 64 to 82% of the protein bands in the incubation medium and the extract have an apparent molecular weight below 50 kDa. An assumption was made about the importance of these proteins in the vital activity of helminths and the need to concentrate further efforts on the study of this particular component of the proteome.

About the authors

T. V. Frolova

Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences

Author for correspondence.
Email: bianka28061981@gmail.com
Russia, Nekouzskii raion, Yaroslavl oblast, Borok

G. I. Izvekova

Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences

Email: bianka28061981@gmail.com
Russia, Nekouzskii raion, Yaroslavl oblast, Borok

References

  1. Извекова Г.И., Фролова Т.И., Жохов А.Е. 2018. Активность протеиназ активность протеиназ в кишечнике ерша Gymnocephalus cernuus (L.) (Pisces) в зависимости от размера населяющих его цестод Proteocephalus cernuae (Gmelin) // Биология внутр. вод. № 1. С. 88. https://doi.org/10.7868/S0320965218010114
  2. Кочнева А.А., Борвинская Е.В., Бедулина Д.С. и др. 2018. Протеомные исследования особенностей жизнедеятельности паразитических червей // Паразитология. Т. 52. № 3. С. 177.
  3. Куперман Б.И. 1988. Функциональная морфология низших цестод. Л.: Наука.
  4. Экологические проблемы Верхней Волги: Коллективная монография. 2001. Ярославль: Изд-во Ярослав. гос.-техн. ун-та.
  5. Barrett J., Precious W.Y. 1995. Application of metabolic control analysis to the pathways of carbohydrate breakdown in Hymenolepis diminuta // Int. J. Parasitol. V. 25. № 4. P. 431. https://doi.org/10.1016/0020-7519(94)00144-D
  6. Bień J., Sałamatin R., Sulima A. et al. 2016. Mass spectrometry analysis of the excretory-secretory (E-S) products of the model cestode Hymenolepis diminuta reveals their immunogenic properties and the presence of new E-S proteins in cestodes // Acta Parasitologica. № 61(2). P. 429. https://doi.org/10.1515/ap-2016-0058
  7. Bosi G., Shinn A.P., Giari L., Dezfuli B.S. 2015. Enteric neuromodulators and mucus discharge in a fish infected with the intestinal helminth Pomphorhynchus laevis // Parasites & Vectors. V. 8. P. 359. https://doi.org/10.1186/s13071-015-0970-7
  8. Bruno R., Maresca M., Canaan S. et al. 2019. Worms’ Antimicrobial Peptides // Marine Drugs. № 17(9). P. 512. https://doi.org/10.3390/md17090512
  9. Dezfuli B.S., Bosi G., DePasquale J.A. et al. 2016. Fish innate immunity against intestinal helminthes // Fish and Shellfish Immunol. V. 50. P. 274. https://doi.org/10.1016/j.fsi.2016.02.002
  10. Dezfuli B.S., Lui A., Giari L. et al. 2013. Piscidins in the intestine of European perch, Perca fluviatilis, naturally infected with an enteric worm // Fish and Shellfish Immunol. V. 35. P. 1539. https://doi.org/10.1016/j.fsi.2013.08.023
  11. Franchini G.R., Pórfido J.L., Shimabukuro M.I. et al. 2015. The unusual lipid binding proteins of parasitic helminthes and their potential roles in parasitism and as therapeutic targets // Prostaglandins, Leukotrienes and Essential Fatty Acids. V. 93. P. 31. https://doi.org/10.1016/j.plefa.2014.08.003
  12. Frolova T.V., Izvekov E.I., Solovyev M.M., Izvekova G.I. 2019. Activity of proteolytic enzymes in the intestine of bream Abramis brama infected with cestodes Caryophyllaeus laticeps (Cestoda, Caryophyllidea) // Comp. Biochem. and Physiol. Part B. V. 235. P. 38. https://doi.org/10.1016/j.cbpb.2019.05.009
  13. Huang S.-Y., Yue D.-M., Hou J.-L. et al. 2019. Proteomic analysis of Fasciola gigantica excretory and secretory products (FgESPs) interacting with buffalo serum of different infection periods by shotgun LC-MS/MS // Parasitol. Res. V. 118. P. 453. https://doi.org/10.1007/s00436-018-6169-z
  14. Izvekova G.I., Frolova T.V., Izvekov E.I. 2017. Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda) // Helminthologia. V. 54(1). P. 3. https://doi.org/10.1515/helm-2017-0001
  15. Frolova T.V., Izvekova G.I. 2022. A Comparative Analysis of the Effect of Intestinal Cestodes in Different Fish Species on Proteolytic Enzyme Activity // J. Evol. Biochem. Physiol. V. 58. №. 3. P. 644. https://doi.org/10.1134/S0022093022030024
  16. Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage // Nature. V. 4(227). № 5259. P. 680.
  17. Molehin A.J., Gobert G.N., McManus D.P. 2012. Serine protease inhibitors of parasitic helminthes // Parasitology. V. 139. № 6. P. 681. https://doi.org/10.1017/S0031182011002435
  18. Oaks J., Knowles W., Cain G. 1977. Simple method of obtaining an enriched fraction of tegumental brush border from Hymenolepis diminuta // J. Parasitol. V. 63. № 3. P. 476. https://doi.org/10.2307/3280005
  19. Pakchotanon P., Molee P., Nuamtanong S. et al. 2016. Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni // Parasitol. Res. V. 115. № 8. P. 2981. https://doi.org/10.1007/s00436-016-5053-y
  20. Ranganathan S., Garg G. 2009. Secretome: clues into pathogen infection and clinical applications // Genome Medicine. V. 1. P. 113. https://doi.org/10.1186/gm113
  21. Rawlings N.D., Tolle D.P., Barrett A.J. 2004. Evolutionary families of peptidase inhibitors // Biochem. J. V. 378. P. 705. https://doi.org/10.1042/BJ20031825
  22. Scholz T. 1999. Life cycles of species of Proteocephalus, parasites of fishes in the Palearctic Region: a review // J. Helminthol. V. 73. № 1. P. 1. https://doi.org/10.1017/S0022149X99000013
  23. Silphaduang U., Colorni A., Noga E.J. 2006. Evidence for widespread distribution of piscidin antimicrobial peptides in teleost fish // Diseases of aquatic organisms. V. 72(3). P. 241. https://doi.org/10.3354/dao072241
  24. Smith V.J., Desbois A.P., Dyrynda E.A. 2010. Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae // Marine Drugs. V. 8. P. 1213. https://doi.org/10.3390/md8041213
  25. Solovyev M.M., Gisbert E. 2016. Influence of time, storage temperature and freeze/thaw cycles on the activity of digestive enzymes from gilthead sea bream (Sparus aurata) // Fish Physiol. and Biochem. V. 42. P. 1383. https://doi.org/10.1007/s10695-016-0226-2
  26. Tassanakajon A., Somboonwiwat K., Amparyup P. 2015. Sequence diversity and evolution of antimicrobial peptides in invertebrates // Devel. and Comp. Immunol. V. 48. P. 324. https://doi.org/10.1016/j.dci.2014.05.020
  27. Zasloff M. 2002. Antimicrobial peptides of multicellular organisms // Nature. V. 415(6870). P. 389. https://doi.org/10.1038/415389a

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2.

Download (167KB)
Indexing metadata
3.

Download (320KB)
Indexing metadata
4.

Download (327KB)
Indexing metadata
5.

Download (149KB)
Indexing metadata

Copyright (c) 2023 Т.В. Фролова, Г.И. Извекова