Publication: Evaluation of rhophilin associated tail protein (Ropn1l) in the human liver fluke opisthorchis viverrini for diagnostic approach
Issued Date
2020-08-01
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17380006
00234001
00234001
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2-s2.0-85089852939
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Mahidol University
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SCOPUS
Bibliographic Citation
Korean Journal of Parasitology. Vol.58, No.4 (2020), 475-479
Suggested Citation
Amornrat Geadkaew-Krenc, Rudi Grams, Wansika Phadungsil, Wanlapa Chaibangyang, Nanthawat Kosa, Poom Adisakwattana, Paron Dekumyoy Evaluation of rhophilin associated tail protein (Ropn1l) in the human liver fluke opisthorchis viverrini for diagnostic approach. Korean Journal of Parasitology. Vol.58, No.4 (2020), 475-479. doi:10.3347/kjp.2020.58.4.475 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/59126
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Title
Evaluation of rhophilin associated tail protein (Ropn1l) in the human liver fluke opisthorchis viverrini for diagnostic approach
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Abstract
© 2020, Korean Society for Parasitology and Tropical Medicine. Tegumental and excretory-secretory proteins are reported as diagnostic antigens for human opisthorchiasis. Rhophilin associated tail protein1-like (OvROPN1L) protein of Opisthorchis viverrini sperm tail showed potential as a diagnostic antigen. The OvROPN1L recombinant fragments were assayed for diagnostic antigenicity for human opisthorchiasis using indirect ELISA. The strongest antigenic region was a N-terminus peptide of M1-P56. One synthetic peptide (P1, L3-Q13) of this region showed the highest antigenicity to opisthorchiasis. Sera from other parasitic infections including Strongyloides stercoralis, hookworm, Taenia spp, minute intestinal flukes, Paragonimus spp showed lower reactivity to P1. Peptide P1 is located in the disordered N-terminus of ROPN1L supporting its suitability as linear epitope. In the Platyhelminthes the N-terminal sequence of ROPN1L is diverging with taxonomic distance further suggesting that peptide P1 has potential as diagnostic tool in the genus Opisthorchis/Clonorchis. It should be further evaluated in combination with peptides derived from other O. viverrini antigens to increase its diagnostic power.