Parasites, Hosts and Diseases

"Nanthawat Kosa"

Brief Communications

Evaluation of Rhophilin Associated Tail Protein (ROPN1L) in the Human Liver Fluke Opisthorchis viverrini for Diagnostic Approach: Amornrat Geadkaew-Krenc, Rudi Grams, Wansika Phadungsil, Wanlapa Chaibangyang, Nanthawat Kosa, Poom Adisakwattana, Paron Dekumyoy; Korean J Parasitol 2020;58(4):475-479.
Published online August 25, 2020; DOI: https://doi.org/10.3347/kjp.2020.58.4.475

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.

Citations

Citations to this article as recorded by

Production and immunological characterization of the novel single-chain variable fragment (scFv) antibodies against the epitopes on Opisthorchis viverrini cathepsin F (OvCatF)
Pongsakorn Martviset, Jeeraphong Thanongsaksrikul, Amornrat Geadkaew-Krenc, Salisa Chaimon, Kantaphon Glab-ampai, Wanlapa Chaibangyang, Phornphan Sornchuer, Potjanee Srimanote, Jittiporn Ruangtong, Parisa Prathaphan, Tonkla Taechadamrongtham, Nattaya Toru
Acta Tropica.2024; 254: 107199. CrossRef
Investigation of a Serine Protease Inhibitor Active in the Infectious Stage of the Human Liver Fluke Opisthorchis viverrini
Rosnanee Salang, Wansika Phadungsil, Amornrat Geadkaew-Krenc, Rudi Grams
Pathogens.2024; 13(8): 678. CrossRef
Production and Immunological Characterization of scFv Specific to Epitope of Opisthorchis viverrini Rhophilin-Associated Tail Protein 1-like (OvROPN1L)
Amornrat Geadkaew-Krenc, Dawid Krenc, Jeeraphong Thanongsaksrikul, Rudi Grams, Wansika Phadungsil, Kittirat Glab-ampai, Pathanin Chantree, Pongsakorn Martviset
Tropical Medicine and Infectious Disease.2023; 8(3): 160. CrossRef
Cystatins from the Human Liver Fluke Opisthorchis viverrini: Molecular Characterization and Functional Analysis
Amornrat Geadkaew-Krenc, Rudi Grams, Sinee Siricoon, Nanthawat Kosa, Dawid Krenc, Wansika Phadungsil, Pongsakorn Martviset
Pathogens.2023; 12(7): 949. CrossRef
Novel recombinant proteins and peptides from Clonorchis sinensis and Opisthorchis viverrini for liver fluke exposure ELISA
Sumathy Mohan, Mohan Natarajan, John G. Bruno
Biochemistry and Biophysics Reports.2023; 35: 101516. CrossRef
Screening of sperm antigen epitopes by phage display technique and its preliminary clinical application
Jin-Chun Lu, Yan-Mei Ge, Yuan-Hua Xu, Shan-Shan Tang, Yuan-Jiao Liang
Basic and Clinical Andrology.2022;[Epub] CrossRef

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Comparative Characterization of Four Calcium-Binding EF Hand Proteins from Opisthorchis viverrini: Palida Emmanoch, Nanthawat Kosa, Suksiri Vichasri-Grams, Smarn Tesana, Rudi Grams, Amornrat Geadkaew-Krenc; Korean J Parasitol 2018;56(1):81-86.
Published online February 28, 2018; DOI: https://doi.org/10.3347/kjp.2018.56.1.81

Four isoforms of calcium binding proteins containing 2 EF hand motifs and a dynein light chain-like domain in the human liver fluke Opisthorchis viverrini, namely OvCaBP1, 2, 3, and 4, were characterized. They had molecular weights of 22.7, 21.6, 23.7, and 22.5 kDa, respectively and showed 37.2-42.1% sequence identity to CaBP22.8 of O. viverrini. All were detected in 2- and 4-week-old immature and mature parasites. Additionally, OvCaBP4 was found in newly excysted juveniles. Polyclonal antibodies against each isoform were generated to detect the native proteins in parasite extracts by Western blot analysis. All OvCaBPs were detected in soluble and insoluble crude worm extracts and in the excretory-secretory product, at approximate sizes of 21-23 kDa. The ion-binding properties of the proteins were analyzed by mobility shift assays with the divalent cations Ca²⁺, Mg²⁺, Zn²⁺, and Cu²⁺. All OvCaBPs showed mobility shifts with Ca²⁺ and Zn²⁺. OvCaBP1 showed also positive results with Mg²⁺ and Cu²⁺. As tegumental proteins, OvCaBP1, 2, and 3 are interesting drug targets for the treatment of opisthorchiasis.

Citations

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Evolutionary analysis of species-specific duplications in flatworm genomes
Mauricio Langleib, Javier Calvelo, Alicia Costábile, Estela Castillo, José F. Tort, Federico G. Hoffmann, Anna V. Protasio, Uriel Koziol, Andrés Iriarte
Molecular Phylogenetics and Evolution.2024; 199: 108141. CrossRef
Cystatins from the Human Liver Fluke Opisthorchis viverrini: Molecular Characterization and Functional Analysis
Amornrat Geadkaew-Krenc, Rudi Grams, Sinee Siricoon, Nanthawat Kosa, Dawid Krenc, Wansika Phadungsil, Pongsakorn Martviset
Pathogens.2023; 12(7): 949. CrossRef
Fasciola gigantica tegumental calcium-binding EF-hand protein 4 exerts immunomodulatory effects on goat monocytes
Muhammad Ehsan, Rui-Si Hu, Jun-Ling Hou, Hany M. Elsheikha, Xiao-Dong Li, Pan-Hong Liang, Xing-Quan Zhu
Parasites & Vectors.2021;[Epub] CrossRef