A rumen fluke Fischoederius elongatus is assigned to the type species of genus Fischoederius, family Gastrothylacidae. However, the mitochondrial sequences recently published are thought to be of inconsistent species, suggesting that several morphologically similar but genetically distinct species might be classified as Fischoederius elongatus. Thus, mentions of F. elongatus from South, Southeast, and East Asia might unintentionally refer to different species. The present work describes morphology and a full mitochondrial genome sequence of one of these species. The fluke specimens were collected from 2 infected cattle in Thailand. An interesting finding was the presence of a second tRNA-Asp gene next to a partial ND1 gene. It is suggested that these duplicated sequences are the remnants of non-reciprocal recombination events caused by inverted repeats located between ND2 and ND1 mitochondrial genes.
Citations
Citations to this article as recorded by
Morphological Observation and Detailed Molecular Characterization of Fischoederius elongatus (Digenea: Gastrothylacidae) from the Rumen of Domestic Cattle in Cambodia Chinda Wann, Bengthay Tep, Witaya Suriyasathaporn, Yasuhiro Morita, Vutha Pheng, Satoshi Ohkura, Shuichi Matsuyama, Sho Nakamura, Kei Hayashi Journal of Parasitology.2025;[Epub] CrossRef
The complete mitochondrial genome of Aspidogaster ijimai (Platyhelminthes: Trematoda: Aspidogastrea): gene content and phylogenetic inference D. A. Solodovnik, D. M. Atopkin, A. A. Semenchenko, M. Urabe, S. G. Sokolov Invertebrate Zoology.2025; 22(3): 411. CrossRef
Differentiating paramphistome species in cattle using DNA barcoding coupled with high-resolution melting analysis (Bar-HRM) Kittisak Buddhachat, Sirikhwan Sriuan, Sirapat Nak-on, Thapana Chontananarth Parasitology Research.2023; 122(3): 769. CrossRef
The determination and relationship of four coexisting paramphistomes in perspective of integrative taxonomic investigation Sirapat Nak-on, Thapana Chontananarth Veterinary Parasitology: Regional Studies and Reports.2023; 40: 100849. CrossRef
The DM9 domain is a protein unit of 60-75 amino acids that has been first detected in the fruit fly Drosophila as a repeated motif of unknown function. Recent research on proteins carrying DM9 domains in the mosquito Anopheles gambiae and the oyster Crassostrea gigas indicated an association with the uptake of microbial organisms. Likewise, in the trematode Fasciola gigantica DM9-1 showed intracellular relocalization following microbial, heat and drug stress. In the present research, we show that FgDM9-1 is a lectin with a novel mannose-binding site that has been recently described for the protein CGL1 of Crassostrea gigas. This property allowed FgDM9-1 to agglutinate gram-positive and -negative bacteria with appropriate cell surface glycosylation patterns. Furthermore, FgDM9-1 caused hemagglutination across all ABO blood group phenotypes. It is speculated that the parenchymal located FgDM9-1 has a role in cellular processes that involve the transport of mannose-carrying molecules in the parenchymal cells of the parasite.
Citations
Citations to this article as recorded by
The Calicophoron daubneyi genome provides new insight into mechanisms of feeding, eggshell synthesis and parasite-microbe interactions Shauna M. Clancy, Mark Whitehead, Nicola A. M. Oliver, Kathryn M. Huson, Jake Kyle, Daniel Demartini, Allister Irvine, Fernanda Godoy Santos, Paul-Emile Kajugu, Robert E. B. Hanna, Sharon A. Huws, Russell M. Morphew, J. Herbert Waite, Sam Haldenby, Mark W BMC Biology.2025;[Epub] CrossRef
DM9CP-8 upon binding microbes activates MASPL-1-C3 axis to regulate the mRNA expressions of IL17s in oysters Yinan Li, Jiejie Sun, Wenwen Yang, Yu Liu, Xingye Lian, Lingling Wang, Linsheng Song International Journal of Biological Macromolecules.2025; 302: 140470. CrossRef
The regulation of CgDM9CP-7 for maintaining the homeostasis of hemolymph microbiota in oyster Crassostrea gigas Shuyi Mu, Yinan Li, Shurong Li, Weishuai Shan, Qiuyan Guo, Zihan Wang, Wei Wu, Lingling Wang, Jiejie Sun, Linsheng Song Comparative Immunology Reports.2025; 8: 200225. CrossRef
A novel intracellular signaling pathway elicited by DM9CP-6 regulates immune responses in oysters Jiejie Sun, Yinan Li, Yu Liu, Lingling Wang, Linsheng Song Cell Communication and Signaling.2025;[Epub] CrossRef
A novel DM9-containing protein 7 involved in regulating the expression of CgMyD88 and CgIL-17 in oyster Crassostrea gigas Yinan Li, Xingye Lian, Wenwen Yang, Jinyuan Leng, Jiejie Sun, Yu Liu, Siqi Fan, Lingling Wang, Linsheng Song Developmental & Comparative Immunology.2024; 150: 105076. CrossRef
Mannose oligosaccharide recognition of CGL1, a mannose-specific lectin containing DM9 motifs from Crassostrea gigas, revealed by X-ray crystallographic analysis Tomomitsu Hatakeyama, Kazuki Masuda, Mizuki Kudo, Koshi Tanaka, Ayaka Takeuchi, Hideaki Unno The Journal of Biochemistry.2024; 175(1): 35. CrossRef
Carbohydrate-binding ability of a recombinant protein containing the DM9 motif from Drosophila melanogaster
Tomomitsu Hatakeyama, Fuki Kojima, Issei Ohkawachi, Hitomi Sawai, Hideaki Unno The Journal of Biochemistry.2024; 175(6): 659. CrossRef
CgDM9CP-5-Integrin-MAPK Pathway Regulates the Production of CgIL-17s and Cgdefensins in the Pacific Oyster, Crassostrea gigas
Yu Liu, Weilin Wang, Jiejie Sun, Yinan Li, Shasha Wu, Qing Li, Miren Dong, Lingling Wang, Linsheng Song The Journal of Immunology.2023; 210(3): 245. CrossRef
Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals Tomomitsu Hatakeyama, Hideaki Unno Cells.2023; 12(14): 1814. CrossRef
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
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
Citations to this article as recorded by
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
Calreticulin (CALR), a multifunctional protein thoroughly researched in mammals, comprises N-, P-, and C-domain and has roles in calcium homeostasis, chaperoning, clearance of apoptotic cells, cell adhesion, and also angiogenesis. In this study, the spatial and temporal expression patterns of the Opisthorchis viverrini CALR gene were analyzed, and calcium-binding and chaperoning properties of recombinant O. viverrini CALR (OvCALR) investigated. OvCALR mRNA was detected from the newly excysted juvenile to the mature parasite by RT-PCR while specific antibodies showed a wide distribution of the protein. OvCALR was localized in tegumental cell bodies, testes, ovary, eggs, Mehlis’
gland, prostate gland, and vitelline cells of the mature parasite. Recombinant OvCALR showed an in vitro suppressive effect on the thermal aggregation of citrate synthase. The recombinant OvCALR C-domain showed a mobility shift in native gel electrophoresis in the presence of calcium. The results imply that OvCALR has comparable function to the mammalian homolog as a calcium-binding molecular chaperone. Inferred from the observed strong immunostaining of the reproductive tissues, OvCALR should be important for reproduction and might be an interesting target to disrupt parasite fecundity. Transacetylase activity of OvCALR as reported for calreticulin of Haemonchus contortus could not be observed.
The many faces of parasite calreticulin Diego Esperante, Ana Flisser, Fela Mendlovic Frontiers in Immunology.2023;[Epub] CrossRef
Two calcium‐binding chaperones from the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) involved in diapause Cansu Doğan, Sabine Hänniger, David G. Heckel, Cathy Coutu, Dwayne D. Hegedus, Linda Crubaugh, Russell L. Groves, Şerife Bayram, Umut Toprak Archives of Insect Biochemistry and Physiology.2021;[Epub] CrossRef
Trypanosoma cruzi Calreticulin: Immune Evasion, Infectivity, and Tumorigenesis Galia Ramírez-Toloza, Eduardo Sosoniuk-Roche, Carolina Valck, Lorena Aguilar-Guzmán, Viviana P. Ferreira, Arturo Ferreira Trends in Parasitology.2020; 36(4): 368. CrossRef
The Interactions of Parasite Calreticulin With Initial Complement Components: Consequences in Immunity and Virulence Galia Ramírez-Toloza, Lorena Aguilar-Guzmán, Carolina Valck, Viviana P. Ferreira, Arturo Ferreira Frontiers in Immunology.2020;[Epub] CrossRef
Diallyl disulfide down‐regulates calreticulin and promotes C/EBPα expression in differentiation of human leukaemia cells Jing Sun, Hongxiang Mu, Jia Yu, Linwei Li, Hongxia Yan, Guoqing Li, Hui Tan, Nanyang Yang, Xiaoyan Yang, Lan Yi Journal of Cellular and Molecular Medicine.2019; 23(1): 194. CrossRef
Evaluation of Opisthorchis viverrini calreticulin for potential host modulation Wanlapa Chaibangyang, Amornrat Geadkaew-Krenc, Peter M. Smooker, Smarn Tesana, Rudi Grams Acta Tropica.2018; 187: 175. CrossRef
First
Prev
