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"Jeong-Hyun Park"

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"Jeong-Hyun Park"

Original Articles

Performance Evaluation of Biozentech Malaria Scanner in Plasmodium knowlesi and P. falciparum as a New Diagnostic Tool
Egy Rahman Firdaus, Ji-Hoon Park, Fauzi Muh, Seong-Kyun Lee, Jin-Hee Han, Chae-Seung Lim, Sung-Hun Na, Won Sun Park, Jeong-Hyun Park, Eun-Taek Han
Korean J Parasitol 2021;59(2):113-119.
Published online April 22, 2021
DOI: https://doi.org/10.3347/kjp.2021.59.2.113
The computer vision diagnostic approach currently generates several malaria diagnostic tools. It enhances the accessible and straightforward diagnostics that necessary for clinics and health centers in malaria-endemic areas. A new computer malaria diagnostics tool called the malaria scanner was used to investigate living malaria parasites with easy sample preparation, fast and user-friendly. The cultured Plasmodium parasites were used to confirm the sensitivity of this technique then compared to fluorescence-activated cell sorting (FACS) analysis and light microscopic examination. The measured percentage of parasitemia by the malaria scanner revealed higher precision than microscopy and was similar to FACS. The coefficients of variation of this technique were 1.2-6.7% for Plasmodium knowlesi and 0.3-4.8% for P. falciparum. It allowed determining parasitemia levels of 0.1% or higher, with coefficient of variation smaller than 10%. In terms of the precision range of parasitemia, both high and low ranges showed similar precision results. Pearson’s correlation test was used to evaluate the correlation data coming from all methods. A strong correlation of measured parasitemia (r2=0.99, P<0.05) was observed between each method. The parasitemia analysis using this new diagnostic tool needs technical improvement, particularly in the differentiation of malaria species.

Citations

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  • In-depth biological analysis of alteration in Plasmodium knowlesi-infected red blood cells using a noninvasive optical imaging technique
    Moh Egy Rahman Firdaus, Fauzi Muh, Ji-Hoon Park, Seong-Kyun Lee, Sung-Hun Na, Won-Sun Park, Kwon-Soo Ha, Jin-Hee Han, Eun-Taek Han
    Parasites & Vectors.2022;[Epub]     CrossRef
  • 5,875 View
  • 151 Download
  • 2 Web of Science
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Characterization of Pv92, a Novel Merozoite Surface Protein of Plasmodium vivax
Seong-Kyun Lee, Bo Wang, Jin-Hee Han, Myat Htut Nyunt, Fauzi Muh, Patchanee Chootong, Kwon-Soo Ha, Won Sun Park, Seok-Ho Hong, Jeong-Hyun Park, Eun-Taek Han
Korean J Parasitol 2016;54(4):385-391.
Published online August 31, 2016
DOI: https://doi.org/10.3347/kjp.2016.54.4.385
The discovery and understanding of antigenic proteins are essential for development of a vaccine against malaria. In Plasmodium falciparum, Pf92 have been characterized as a merozoite surface protein, and this protein is expressed at the late schizont stage, but no study of Pv92, the orthologue of Pf92 in P. vivax, has been reported. Thus, the protein structure of Pv92 was analyzed, and the gene sequence was aligned with that of other Plasmodium spp. using bioinformatics tools. The recombinant Pv92 protein was expressed and purified using bacterial expression system and used for immunization of mice to gain the polyclonal antibody and for evaluation of antigenicity by protein array. Also, the antibody against Pv92 was used for subcellular analysis by immunofluorescence assay. The Pv92 protein has a signal peptide and a sexual stage s48/45 domain, and the cysteine residues at the N-terminal of Pv92 were completely conserved. The N-terminal of Pv92 was successfully expressed as soluble form using a bacterial expression system. The antibody raised against Pv92 recognized the parasites and completely merged with PvMSP1-19, indicating that Pv92 was localized on the merozoite surface. Evaluation of the human humoral immune response to Pv92 indicated moderate antigenicity, with 65% sensitivity and 95% specificity by protein array. Taken together, the merozoite surface localization and antigenicity of Pv92 implicate that it might be involved in attachment and invasion of a merozoite to a new host cell or immune evasion during invasion process.

Citations

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  • Merozoite surface protein 1 paralog is involved in the human erythrocyte invasion of a zoonotic malaria, Plasmodium knowlesi
    Seong-Kyun Lee, Tuyet Kha Nguyen, Franziska Mohring, Jin-Hee Han, Egy Rahman Firdaus, Sung-Hun Na, Won-Sun Park, Robert W. Moon, Eun-Taek Han
    Frontiers in Cellular and Infection Microbiology.2023;[Epub]     CrossRef
  • A novel platform for peptide-mediated affinity capture and LC-MS/MS identification of host receptors involved in Plasmodium invasion
    Jessica Molina-Franky, David Fernando Plaza, Carmen Merali, Salim Merali, Carlos Barrero, Gabriela Arévalo-Pinzón, Manuel Elkin Patarroyo, Manuel Alfonso Patarroyo
    Journal of Proteomics.2021; 231: 104002.     CrossRef
  • Inhibition of parasite invasion by monoclonal antibody against epidermal growth factor-like domain of Plasmodium vivax merozoite surface protein 1 paralog
    Jin-Hee Han, Yang Cheng, Fauzi Muh, Md Atique Ahmed, Jee-Sun Cho, Myat Htut Nyunt, Hye-Yoon Jeon, Kwon-Soo Ha, Sunghun Na, Won Sun Park, Seok-Ho Hong, Ho-Joon Shin, Bruce Russell, Eun-Taek Han
    Scientific Reports.2019;[Epub]     CrossRef
  • Plasmodium vivax in vitro continuous culture: the spoke in the wheel
    Maritza Bermúdez, Darwin Andrés Moreno-Pérez, Gabriela Arévalo-Pinzón, Hernando Curtidor, Manuel Alfonso Patarroyo
    Malaria Journal.2018;[Epub]     CrossRef
  • 10,537 View
  • 257 Download
  • 4 Web of Science
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Identification of Immunodominant B-cell Epitope Regions of Reticulocyte Binding Proteins in Plasmodium vivax by Protein Microarray Based Immunoscreening
Jin-Hee Han, Jian Li, Bo Wang, Seong-Kyun Lee, Myat Htut Nyunt, Sunghun Na, Jeong-Hyun Park, Eun-Taek Han
Korean J Parasitol 2015;53(4):403-411.
Published online August 25, 2015
DOI: https://doi.org/10.3347/kjp.2015.53.4.403
Plasmodium falciparum can invade all stages of red blood cells, while Plasmodium vivax can invade only reticulocytes. Although many P. vivax proteins have been discovered, their functions are largely unknown. Among them, P. vivax reticulocyte binding proteins (PvRBP1 and PvRBP2) recognize and bind to reticulocytes. Both proteins possess a C-terminal hydrophobic transmembrane domain, which drives adhesion to reticulocytes. PvRBP1 and PvRBP2 are large (> 326 kDa), which hinders identification of the functional domains. In this study, the complete genome information of the P. vivax RBP family was thoroughly analyzed using a prediction server with bioinformatics data to predict B-cell epitope domains. Eleven pvrbp family genes that included 2 pseudogenes and 9 full or partial length genes were selected and used to express recombinant proteins in a wheat germ cell-free system. The expressed proteins were used to evaluate the humoral immune response with vivax malaria patients and healthy individual serum samples by protein microarray. The recombinant fragments of 9 PvRBP proteins were successfully expressed; the soluble proteins ranged in molecular weight from 16 to 34 kDa. Evaluation of the humoral immune response to each recombinant PvRBP protein indicated a high antigenicity, with 38-88% sensitivity and 100% specificity. Of them, N-terminal parts of PvRBP2c (PVX_090325-1) and PvRBP2 like partial A (PVX_090330-1) elicited high antigenicity. In addition, the PvRBP2-like homologue B (PVX_116930) fragment was newly identified as high antigenicity and may be exploited as a potential antigenic candidate among the PvRBP family. The functional activity of the PvRBP family on merozoite invasion remains unknown.

Citations

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  • Alternative Invasion Mechanisms and Host Immune Response to Plasmodium vivax Malaria: Trends and Future Directions
    Daniel Kepple, Kareen Pestana, Junya Tomida, Abnet Abebe, Lemu Golassa, Eugenia Lo
    Microorganisms.2020; 9(1): 15.     CrossRef
  • Epitope-Based Vaccine Designing of Nocardia asteroides Targeting the Virulence Factor Mce-Family Protein by Immunoinformatics Approach
    Prasanta Patra, Niladri Mondal, Bidhan Chandra Patra, Manojit Bhattacharya
    International Journal of Peptide Research and Therapeutics.2020; 26(2): 1165.     CrossRef
  • Plasmodium vivax Reticulocyte Binding Proteins for invasion into reticulocytes
    Li‐Jin Chan, Melanie H. Dietrich, Wang Nguitragool, Wai‐Hong Tham
    Cellular Microbiology.2020;[Epub]     CrossRef
  • From a basic to a functional approach for developing a blood stage vaccine against Plasmodium vivax
    Manuel Alfonso Patarroyo, Gabriela Arévalo-Pinzón, Darwin A. Moreno-Pérez
    Expert Review of Vaccines.2020; 19(2): 195.     CrossRef
  • Inferring Plasmodium vivax protein biology by using omics data
    D.A. Moreno-Pérez, M.A. Patarroyo
    Journal of Proteomics.2020; 218: 103719.     CrossRef
  • Prediction of B cell and T‐helper cell epitopes candidates of bovine leukaemia virus (BLV) by in silico approach
    Negar Hooshmand, Jamal Fayazi, Saleh Tabatabaei, Nader Ghaleh Golab Behbahan
    Veterinary Medicine and Science.2020; 6(4): 730.     CrossRef
  • Serodiagnostic antigens of Clonorchis sinensis identified and evaluated by high-throughput proteogenomics
    Pyo Yun Cho, Ji-Yun Lee, Tae Im Kim, Jin-Ho Song, Sung-Jong Hong, Won Gi Yoo, Takafumi Tsuboi, Kwon-Soo Ha, Jae-Wan Jung, Satoru Takeo, Eun-Taek Han, Banchob Sripa, Sung-Tae Hong, Jong-Yil Chai, Ho-Woo Nam, Jhang Ho Pak, Tong-Soo Kim, Krystyna Cwiklinski
    PLOS Neglected Tropical Diseases.2020; 14(12): e0008998.     CrossRef
  • Contribution ofPlasmodiumimmunomics: potential impact for serological testing and surveillance of malaria
    Kokouvi Kassegne, Eniola Michael Abe, Yan-Bing Cui, Shen-Bo Chen, Bin Xu, Wang-Ping Deng, Hai-Mo Shen, Yue Wang, Jun-Hu Chen, Xiao-Nong Zhou
    Expert Review of Proteomics.2019; 16(2): 117.     CrossRef
  • Identification and Immunological Characterization of the Ligand Domain of Plasmodium vivax Reticulocyte Binding Protein 1a
    Francis B Ntumngia, Richard Thomson-Luque, Sandra Galusic, Gabriel Frato, Sarah Frischmann, David S Peabody, Bryce Chackerian, Marcelo U Ferreira, Christopher L King, John H Adams
    The Journal of Infectious Diseases.2018; 218(7): 1110.     CrossRef
  • Plasmodium vivax vaccine research – we’ve only just begun
    Wai-Hong Tham, James G. Beeson, Julian C. Rayner
    International Journal for Parasitology.2017; 47(2-3): 111.     CrossRef
  • What Is Known about the Immune Response Induced by Plasmodium vivax Malaria Vaccine Candidates?
    Carolina López, Yoelis Yepes-Pérez, Natalia Hincapié-Escobar, Diana Díaz-Arévalo, Manuel A. Patarroyo
    Frontiers in Immunology.2017;[Epub]     CrossRef
  • Identification of a reticulocyte-specific binding domain of Plasmodium vivax reticulocyte-binding protein 1 that is homologous to the PfRh4 erythrocyte-binding domain
    Jin-Hee Han, Seong-Kyun Lee, Bo Wang, Fauzi Muh, Myat Htut Nyunt, Sunghun Na, Kwon-Soo Ha, Seok-Ho Hong, Won Sun Park, Jetsumon Sattabongkot, Takafumi Tsuboi, Eun-Taek Han
    Scientific Reports.2016;[Epub]     CrossRef
  • Plasmodium vivax GPI-anchored micronemal antigen (PvGAMA) binds human erythrocytes independent of Duffy antigen status
    Yang Cheng, Feng Lu, Bo Wang, Jian Li, Jin-Hee Han, Daisuke Ito, Deok-Hoon Kong, Lubin Jiang, Jian Wu, Kwon-Soo Ha, Eizo Takashima, Jetsumon Sattabongkot, Jun Cao, Myat Htut Nyunt, Myat Phone Kyaw, Sanjay A. Desai, Louis H. Miller, Takafumi Tsuboi, Eun-Ta
    Scientific Reports.2016;[Epub]     CrossRef
  • Plasmodium vivax Reticulocyte Binding Proteins Are Key Targets of Naturally Acquired Immunity in Young Papua New Guinean Children
    Camila T. França, Wen-Qiang He, Jakub Gruszczyk, Nicholas T. Y. Lim, Enmoore Lin, Benson Kiniboro, Peter M. Siba, Wai-Hong Tham, Ivo Mueller, Henk D. F. H. Schallig
    PLOS Neglected Tropical Diseases.2016; 10(9): e0005014.     CrossRef
  • Gene Models, Expression Repertoire, and Immune Response of Plasmodium vivax Reticulocyte Binding Proteins
    Jenni Hietanen, Anongruk Chim-ong, Thanprakorn Chiramanewong, Jakub Gruszczyk, Wanlapa Roobsoong, Wai-Hong Tham, Jetsumon Sattabongkot, Wang Nguitragool, J. H. Adams
    Infection and Immunity.2016; 84(3): 677.     CrossRef
  • 12,027 View
  • 153 Download
  • 16 Web of Science
  • Crossref
Brief Communications
Metagonimus yokogawai: a 100-kDa Somatic Antigen Commonly Reacting with Other Trematodes
Eun-Taek Han, Hyun-Jong Yang, Young-Jin Park, Jeong-Hyun Park, Jong-Yil Chai
Korean J Parasitol 2014;52(2):201-204.
Published online April 18, 2014
DOI: https://doi.org/10.3347/kjp.2014.52.2.201

This study was undertaken to characterize the properties of a 100 kDa somatic antigen from Metagonimus yokogawai. Monoclonal antibodies (mAbs) were produced against this 100 kDa antigen, and their immunoreactivity was assessed by western blot analysis with patients' sera. The mAbs against the 100 kDa antigen commonly reacted with various kinds of trematode antigens, including intestinal (Gymnophalloides seoi), lung (Paragonimus westermani), and liver flukes (Clonorchis sinensis and Fasciola hepatica). However, this mAb showed no cross-reactions with other helminth parasites, including nematodes and cestodes. To determine the topographic distribution of the 100 kDa antigen in worm sections, indirect immunoperoxidase staining was performed. A strong positive reaction was observed in the tegumental and subtegumental layers of adult M. yokogawai and C. sinensis. The results showed that the 100 kDa somatic protein of M. yokogawai is a common antigen which recognizes a target epitope present over the tegumental layer of different trematode species.

Citations

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  • Reliability of heterophyid antigens in heterologous protection against human schistosomiasis
    Alaa H. A. Hegazy, Lamia A. Galal, Tasneem M. Hassan, Refaat M. A. Khalifa
    Journal of Parasitic Diseases.2020; 44(2): 349.     CrossRef
  • Fishborne zoonotic heterophyid infections: An update
    Jong-Yil Chai, Bong-Kwang Jung
    Food and Waterborne Parasitology.2017; 8-9: 33.     CrossRef
  • 8,993 View
  • 84 Download
  • 3 Web of Science
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Cercaria caribbea LVIII Cable, 1963 (Digenea: Cyathocotylidae) in the Republic of Korea and Its Surface Ultrastructure
Eun-Taek Han, Jeong-Hyun Park, Jong-Yil Chai
Korean J Parasitol 2012;50(2):177-180.
Published online May 24, 2012
DOI: https://doi.org/10.3347/kjp.2012.50.2.177

Cercaria caribbea LVIII Cable, 1963 (Digenea: Cyathocotylidae) was detected from a brackish water gastropod species (Cerithideopsilla cingulata) in a coatal area of Shinan-gun, Jeollanam-do (Province), the Republic of Korea, and its surface ultrastructure was studied using a scanning electron microscope. The cercariae were found freely swimming or enveloped within daughter sporocysts when the snail host was mechanically broken. They were morphologically characterized by a linguiform and ventrally concave body, a long and bifurcated tail, and the presence of a holdfast (=tribocytic) organ posterior to the ventral sucker. On the whole ventral and dorsal surfaces, peg-like tegumental spines were densely distributed. Around the oral sucker, several sensory papillae, each with a short cilium, were distributed, and on the tail, sensory papillae, each with an extensively long cilium, were observed. This is the first record describing a cyathocotylid cercaria from a brackish water gastropod in the Republic of Korea.

Citations

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  • A preliminary study on some larval trematodes parasites of marine snail Cerithidea cingulata (Gmelin, 1791) in Al- faw Bay, South of Iraq

    International Journal of Biosciences (IJB).2020; : 464.     CrossRef
  • 7,977 View
  • 87 Download
  • Crossref