Protozoan parasites such as Eimeria tenella and Toxoplasma gondii pose significant health challenges in livestock and humans. The limited treatment options and rising drug resistance underscore the urgent need for new therapies. This study investigates myrcene, a monoterpene hydrocarbon classified for its antiprotozoal potential against E. tenella and T. gondii infections. Initially, we examined its effect on the sporulation process of E. tenella oocysts in vitro and its anti-E. tenella activity in vivo. Myrcene significantly reduced the sporulation rate of E. tenella oocysts at 3 and 4 mg/kg. In vivo experiments demonstrated that treatment with 4 mg/kg myrcene significantly reduced E. tenella load and oocyst output, as well as cecal lesion and weight loss caused by E. tenella infection, showing moderate anti-E. tenella activity, with an Anticoccidial Index (ACI) of 161.4. Furthermore, we investigated the anti-T. gondii activity of myrcene both in vitro and in vivo. In vitro studies showed that treatment with myrcene effectively inhibited the invasion rate and intracellular proliferation ability of T. gondii tachyzoite in DF-1 cells in a dose-dependent manner. In vivo administration prolonged the survival time in T. gondii-infected mice, suggesting notable protective effects. Additionally, it mitigated T. gondii-induced hepatosplenic toxicity by reducing parasite load in the liver and spleen, and ameliorating liver function as evidenced by decreased serum transaminase levels. In conclusion, the findings demonstrate promising anti-E. tenella and anti-T. gondii activity exhibited by myrcene warranting further exploration into its mechanisms and potential therapeutic applications.
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http://dx.doi.org/10.1292/jvms.24-0397 | DOI Listing |
J Vet Med Sci
November 2024
Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Shandong Agricultural University.
Protozoan parasites such as Eimeria tenella and Toxoplasma gondii pose significant health challenges in livestock and humans. The limited treatment options and rising drug resistance underscore the urgent need for new therapies. This study investigates myrcene, a monoterpene hydrocarbon classified for its antiprotozoal potential against E.
View Article and Find Full Text PDFFront Cell Infect Microbiol
July 2023
College of Animal & Veterinary Sciences, Southwest Minzu University, Chengdu, Sichuan, China.
Introduction: Vacuolar protein sorting 29 (VPS29) is a core component of the retromer-retriever complex and is essential for recycling numerous cell-surface cargoes from endosomes. However, there are no reports yet on VPS29 of spp.
Methods: Here, we cloned and prokaryotically expressed a partial sequence of VPS29 (EtVPS29) with RT-PCR and engineered strain of respectively.
Parasitol Res
September 2010
Institute of Parasitology, Faculty of Veterinary Medicine, University of Leipzig, Leipzig, Germany.
Coccidiosis in chicken causes great economic losses. The increasing resistance of Eimeria species to anticoccidials has induced the search for alternative methods of control. In vivo antibody neutralization assay was conducted to study the inhibitory effect of nine antibody fragments (Ab1-Ab9) on Eimeria tenella sporozoites.
View Article and Find Full Text PDFAvian Pathol
December 1995
Department of Veterinary Microbiology and Parasitology, Faculty of Veterinary Medicine, UCD, Dublin 4, Ireland.
SDS-PAGE fingerprint studies of oocyst antigens of five major Eimeria species including E. acervulina, E. maxima, E.
View Article and Find Full Text PDFInfect Immun
October 1994
Department of Veterinary Microbiology and Parasitology, University College Dublin, Ireland.
Overlapping hexapeptides representing part of an Eimeria tenella antigenic sequence, shown to induce partial immunity to homologous challenge in chickens, were synthesized on polypropylene pins (Pepskan technique; Cambridge Research Biochemicals, Cambridge, United Kingdom). The binding to these hexapeptides of antibodies from chickens infected and rabbits immunized with five species of Eimeria was studied, using the coated pins as the solid phase of an enzyme-linked immunoassay. Antibody binding to most regions of the sequence was demonstrated, with peak areas of antigenicity correlating with the most hydrophilic regions.
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