Characterization of benzimidazole resistance in Haemonchus contortus: integration of phenotypic, genotypic and proteomic approaches
| Autor: | Kek Heng Chua, Premaalatha Bathmanaban, Yvonne A. L. Lim, Tiong Kai Tan, Hwa Chia Chai, Sarah Affendi, Daryi Wang, Chandrawathani Panchadcharam, Van Lun Low |
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| Rok vydání: | 2019 |
| Předmět: |
Proteomics
Benzimidazole Difference gel electrophoresis 030231 tropical medicine Drug Resistance Sheep Diseases Albendazole Malate dehydrogenase Polymerase Chain Reaction Antioxidants 030308 mycology & parasitology 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Glutamate Dehydrogenase Tandem Mass Spectrometry Tubulin medicine Animals Anthelmintic Gene Anthelmintics 0303 health sciences Sheep General Veterinary Strain (chemistry) biology Glutamate dehydrogenase General Medicine biology.organism_classification Infectious Diseases chemistry Biochemistry Insect Science Parasitology Benzimidazoles Haemonchus Haemonchiasis medicine.drug Haemonchus contortus Chromatography Liquid |
| Zdroj: | Parasitology research. 119(9) |
| ISSN: | 1432-1955 |
| Popis: | The field strain of Haemonchus contortus has a long history of anthelmintic resistance. To understand this phenomenon, the benzimidazole resistance profile was characterized from the Malaysian field-resistant strain by integrating phenotypic, genotypic and proteomic approaches. The faecal egg count reduction test (FECRT) demonstrated that benzimidazole resistance was at a critical level in the studied strain. The primary resistance mechanism was attributed to F200Y mutation in the isotype 1 β-tubulin gene as revealed by AS-PCR and direct sequencing. Furthermore, the protein response of the resistant strain towards benzimidazole (i.e., albendazole) treatment was investigated via two-dimensional difference gel electrophoresis (2D-DIGE) and tandem liquid chromatography-mass spectrometry (LC-MS/MS). These investigations illustrated an up-regulation of antioxidant (i.e., ATP-binding region and heat-shock protein 90, superoxide dismutase) and metabolic (i.e., glutamate dehydrogenase) enzymes and down-regulation of glutathione S-transferase, malate dehydrogenase, and other structural and cytoskeletal proteins (i.e., actin, troponin T). Findings from this study are pivotal in updating the current knowledge on anthelmintic resistance and providing new insights into the defence mechanisms of resistant nematodes towards drug treatment. |
| Databáze: | OpenAIRE |
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