Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. multilocularis.
Abstract: Extracts of the horse and sheep strains of Echinococcus granulosus and E. multilocularis were compared on the basis of their isoenzyme patterns for 10 enzymes by means of isoelectric focusing in polyacrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and alpha-glycerophosphate dehydrogenase. Interspecific and intraspecific differences are apparent in the isoenzyme profiles of all the enzymes except adenylate kinase; the pattern and activity of adenylate kinase are identical for both strains of E. granulosus but this enzyme clearly distinguishes these forms from E. multilocularis. The absence of electromorphic variation in any of the enzymes from either form of E. granulosus may be a result of the self-fertilizing hermaphraditism of these organisms.
Publication Date: 1979-01-01 PubMed ID: 473321DOI: 10.1016/0035-9203(79)90079-8Google Scholar: Lookup
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- Journal Article
Summary
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This research investigated the isoenzyme patterns of certain enzymes in the horse and sheep strains of a parasite, Echinococcus granulosus, and E. multilocularis. The results showed that these organisms exhibit distinct isoenzyme profiles, with one enzyme, adenylate kinase, being notably consistent within E. granulosus strains, differentiating them from E. multilocularis.
Research Objectives and Methodology
- The study aimed to compare the molecular structure and function of certain enzymes from two types of Echinococcus, a parasitic worm affecting horses and sheep primarily.
- The method applied was isoelectric focusing in polyacrylamide gels, a technique providing resolution of proteins based on their isoelectric points, to evaluate and differentiate isoenzyme patterns.
- Ten different enzymes were doggedly examined within this study. Notably these included: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, and phosphoglucoseisomerase, among others.
Findings and Conclusions
- The research concluded that there were both interspecific (between different species) and intraspecific (within the same species) differences in the isoenzyme profiles of almost all enzymes, except for adenylate kinase.
- The specific isoenzyme structure and activity of adenylate kinase remained identical in both horse and sheep strains of E. granulosus, successfully differentiating them from E. multilocularis.
- The consistency or lack of variation in any of the enzymes from either form of E. granulosus could possibly be due to their physiological trait of being self-fertilizing hermaphrodites.
- This implies that certain characteristics at the enzymatic level might serve as a reliable identification marker in distinguishing distinct forms or strains of the same parasite species, shaping the future of parasitology and disease diagnosis.
Significance of the Study
- This research contributes to the broader understanding of parasitic organisms and their distinctive enzymatic functions and profiles. Such knowledge can be pivotal in differentiating between similar species or strains, which is crucial in accurate disease diagnosis and treatment.
- Furthermore, the noted consistency in the isoenzyme pattern of adenylate kinase in different strains of E. granulosus may open up possibilities for further research in this area, and potentially pave the way for new diagnostic methods or potential treatments.
Cite This Article
APA
McManus DP, Smyth JD.
(1979).
Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. multilocularis.
Trans R Soc Trop Med Hyg, 73(3), 259-265.
https://doi.org/10.1016/0035-9203(79)90079-8 Publication
Researcher Affiliations
MeSH Terms
- Adenylate Kinase / analysis
- Animals
- Echinococcus / enzymology
- Fructose-Bisphosphate Aldolase / analysis
- Horses / parasitology
- Isoelectric Focusing
- Isoenzymes / analysis
- Sheep / parasitology
- Species Specificity
Citations
This article has been cited 10 times.- Song HY, Zhan JF, Hua RQ, He X, Du XD, Xu J, He R, Xie Y, Gu XB, Peng XR, Yang GY. Molecular characterization and immunological properties of Echinococcus granulosus sensu stricto (G1) ADK1 and ADK8.. Parasitol Res 2023 Jul;122(7):1557-1565.
- Dousti M, Sadjjadi SM, Solgi R, Vafafar A, Sharifi Y, Radfar A, Hatam GR. Comparison of Isoenzyme Pattern of Echinococcus granulosus sensu stricto (G1-G3) and E. canadensis (G6/G7) Protoscoleces.. Iran Biomed J 2023 Mar 1;27(2 & 3):136-45.
- Guo X. Proteomics Analysis of Hydatigera taeniaeformis Metacestode Stage.. Front Vet Sci 2020;7:474.
- Cutillas C, Arias P, Spakulova M. Malic dehydrogenase isoenzymatic pattern in lung-nematode parasite species.. Parasitol Res 1996;82(1):92-4.
- Snábel V, Hanzelová V, Fagerholm HP. Morphological and genetic comparison of two Proteocephalus species (Cestoda: Proteocephalidae).. Parasitol Res 1994;80(2):141-6.
- Kumaratilake LM, Thompson RC. A review of the taxonomy and speciation of the genus Echinococcus Rudolphi 1801.. Z Parasitenkd 1982;68(2):121-46.
- Fukumoto S, Takechi M, Kamo H, Yamaguchi T. Comparative studies on soluble protein profiles and isozyme patterns of seven Trichinella isolates.. Parasitol Res 1987;73(4):352-7.
- Fukumoto S, Nagai D, Yazaki S, Kamo H, Yamaguchi T. The molecular phylogenic tree of the genus Trichinella constructed from isozyme patterns.. Parasitol Res 1988;74(6):574-80.
- Moura H, Wallace S, Visvesvara GS. Acanthamoeba healyi n. sp. and the isoenzyme and immunoblot profiles of Acanthamoeba spp., groups 1 and 3.. J Protozool 1992 Sep-Oct;39(5):573-83.
- Homan WL, van Enckevort FH, Limper L, van Eys GJ, Schoone GJ, Kasprzak W, Majewska AC, van Knapen F. Comparison of Giardia isolates from different laboratories by isoenzyme analysis and recombinant DNA probes.. Parasitol Res 1992;78(4):316-23.
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