Parasites, Hosts and Diseases

"Platyhelminthes"

Brief Communication

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.

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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

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Original Articles

Molecular and Biochemical Characterization of Opisthorchis viverrini Calreticulin: Wanlapa Chaibangyang, Amornrat Geadkaew-Krenc, Suksiri Vichasri-Grams, Smarn Tesana, Rudi Grams; Korean J Parasitol 2017;55(6):643-652.
Published online December 31, 2017; DOI: https://doi.org/10.3347/kjp.2017.55.6.643

Abstract
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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.

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Jing Zhang, Zhenke Yang, Hangbin Ma, Xiaowei Tian, Jiani Li, Zihang Zhang, Longxin Yang, Mengchuang Feng, Xuefang Mei, Zhenchao Zhang, Xingrui Li, Shuai Wang
Acta Tropica.2023; 241: 106883. CrossRef
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
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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
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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

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Molecular phylogeny of parasitic Platyhelminthes based on sequences of partial 28S rDNA D1 and mitochondrial cytochrome c oxidase subunit I: Soo-Ung Lee, Ha-Chung Chun, Sun Huh; Korean J Parasitol 2007;45(3):181-189.
Published online September 20, 2007; DOI: https://doi.org/10.3347/kjp.2007.45.3.181

Abstract
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The phylogenic relationships existing among 14 parasitic Platyhelminthes in the Republic of Korea were investigated via the use of the partial 28S ribosomal DNA (rDNA) D1 region and the partial mitochondrial cytochrome c oxidase subunit 1 (mCOI) DNA sequences. The nucleotide sequences were analyzed by length, G + C %, nucleotide differences and gaps in order to determine the analyzed phylogenic relationships. The phylogenic patterns of the 28S rDNA D1 and mCOI regions were closely related within the same class and order as analyzed by the PAUP 4.0 program, with the exception of a few species. These findings indicate that the 28S rDNA gene sequence is more highly conserved than are the mCOI gene sequences. The 28S rDNA gene may prove useful in studies of the systematics and population genetic structures of parasitic Platyhelminthes.

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Codon usage and bias in mitochondrial genomes of parasitic platyhelminthes: Thanh Hoa Le, Donald Peter McManus, David Blair; Korean J Parasitol 2004;42(4):159-167.
Published online December 20, 2004; DOI: https://doi.org/10.3347/kjp.2004.42.4.159

Abstract
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Sequences of the complete protein-coding portions of the mitochondrial (mt) genome were analysed for 6 species of cestodes (including hydatid tapeworms and the pork tapeworm) and 5 species of trematodes (blood flukes and liver- and lung-flukes). A near-complete sequence was also available for an additional trematode (the blood flukeSchistosoma malayensis). All of these parasites belong to a large flatworm taxon named the Neodermata. Considerable variation was found in the base composition of the protein-coding genes among these neodermatans. This variation was reflected in statistically-significant differences in numbers of each inferred amino acid between many pairs of species. Both convergence and divergence in nucleotide, and hence amino acid, composition was noted among groups within the Neodermata. Considerable variation in skew (unequal representation of complementary bases on the same strand) was found among the species studied. A pattern is thus emerging of diversity in the mt genome in neodermatans that may cast light on evolution of mt genomes generally.

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