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Brief Communication

Specific Detection of Acanthamoeba species using Polyclonal Peptide Antibody Targeting the Periplasmic Binding Protein of A. castellanii
Min-Jeong Kim, Fu-Shi Quan, Hyun-Hee Kong, Jong-Hyun Kim, Eun-Kyung Moon
Korean J Parasitol 2022;60(2):143-147.
Published online April 20, 2022
DOI: https://doi.org/10.3347/kjp.2022.60.2.143
Acanthamoeba keratitis (AK) is a rare ocular disease, but it is a painful and sight-threatening infectious disease. Early diagnosis and adequate treatment are necessary to prevent serious complications. While AK is frequently diagnosis via several PCR assays or Acanthamoeba-specific antibodies, a more specific and effective diagnostic method is required. This study described the production of a polyclonal peptide antibody against the periplasmic binding protein (PBP) of A. castellanii and investigated its diagnostic potential. Western blot analysis showed that the PBP antibody specifically reacted with the cell lysates of A. castellanii. However, the PBP antibody did not interact with human corneal epithelial (HCE) cells and the other 3 major causative agents of keratitis. Immunocytochemistry (ICC) results revealed the specific detection of A. castellanii trophozoites and cysts by PBP antibodies when A. castellanii were co-cultured with HCE cells. PBP antibody specificity was further confirmed by co-culture of A. castellanii trophozoites with F. solani, S. aureus, and P. aeruginosa via ICC. The PBP antibody specifically reacted with the trophozoites and cysts of A. polyphaga, A. hatchetti, A. culbertsoni, A. royreba, and A. healyi, thus demonstrated its genus-specific nature. These results showed that the PBP polyclonal peptide antibody of A. castellanii could specifically detect several species of Acanthamoeba, contributing to the development of an effective antibody-based AK diagnostics.

Citations

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  • Evaluation of the potential for diagnosis of fungal keratitis using a Fusarium-specific antibody
    Hye-Jeong Jo, Min-Jeong Kim, Hae-Ahm Lee, Fu-Shi Quan, Hyun-Hee Kong, Eun-Kyung Moon
    Scientific Reports.2025;[Epub]     CrossRef
  • Detection of Fusarium solani using cutinase antibody and its application in diagnosing fungal keratitis in an animal model
    Hye-Jeong Jo, Min-Jeong Kim, Hae-Ahm Lee, Fu-Shi Quan, Hyun-Hee Kong, Eun-Kyung Moon, Olaf Kniemeyer
    PLOS One.2025; 20(8): e0330455.     CrossRef
  • A chorismate mutase-targeted, core-shell nanoassembly-activated SERS immunoassay platform for rapid non-invasive detection of Acanthamoeba infection
    Hyerin Lee, Min-Jeong Kim, Junkyu Chung, Wansun Kim, Hye-Jeong Jo, Tae Gi Kim, Jae-Ho Shin, Gi-Ja Lee, Fu-Shi Quan, Hyun-Hee Kong, Sang Woong Moon, Eun-Kyung Moon, Samjin Choi
    Nano Today.2024; 59: 102506.     CrossRef
  • Evaluating the Diagnostic Potential of Chorismate Mutase Poly-Clonal Peptide Antibody for the Acanthamoeba Keratitis in an Animal Model
    Min-Jeong Kim, Hye-Jeong Jo, Hae-Jin Sohn, Ho-Joon Shin, Fu-Shi Quan, Hyun-Hee Kong, Eun-Kyung Moon
    Pathogens.2023; 12(4): 526.     CrossRef
  • Detection of Acanthamoeba from Acanthamoeba Keratitis Mouse Model Using Acanthamoeba-Specific Antibodies
    Min-Jeong Kim, A-Jeong Ham, A-Young Park, Hae-Jin Sohn, Ho-Joon Shin, Fu-Shi Quan, Hyun-Hee Kong, Eun-Kyung Moon
    Microorganisms.2022; 10(9): 1711.     CrossRef
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Original Article

Expression of Chicken NK-Lysin and Its Role in Chicken Coccidiosis Induced by Eimeria necatrix
Woo Hyun Kim, Wongi Min, Kwang Il Park, Hyun S. Lillehoj, Cherry P. Fernandez-Colorado, Rochelle A. Flores, Paula Leona T. Cammayo, Binh Thanh Nguyen
Korean J Parasitol 2021;59(5):439-445.
Published online October 22, 2021
DOI: https://doi.org/10.3347/kjp.2021.59.5.439
Coccidiosis in chickens is an intestinal parasitic disease caused by protozoan parasites named Eimeria spp. In some Eimeria infections, intestinal lymphocytes are known to highly express chicken NK-lysin (cNK-lysin), an antimicrobial peptide with anticoccidial activity. Therefore, this study aims to investigate the expression of cNK-lysin in E. necatrix-infected chickens and its role in E. necatrix infection. The expression of cNK-lysin transcript was significantly increased in E. necatrix sporozoites-treated lymphocytes. In E. necatrix infection, cNK-lysin transcript was induced in intestinal lymphocytes but not in the spleen. The recombinant cNK-lysin exhibited anticoccidial activity against E. necatrix sporozoites as well as immunomodulatory activity on macrophages by inducing proinflammatory cytokines. These results indicated that E. necatrix infection induces high local expression of cNK-lysin and the secreted cNK-lysin helps protect coccidiosis.

Citations

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  • Characterization of NK-lysin A, a potent antimicrobial peptide from the zebrafish Danio rerio
    Marius Ortjohann, Matthias Leippe
    Developmental & Comparative Immunology.2025; 162: 105266.     CrossRef
  • Exploring the interplay between Eimeria spp. infection and the host: understanding the dynamics of gut barrier function
    Pan Chen, Mujeeb Ur Rehman, Yanfeng He, Aoyun Li, Fuchun Jian, Longxian Zhang, Shucheng Huang
    Veterinary Quarterly.2025; 45(1): 1.     CrossRef
  • Development and immunological insights into recombinant/subunit vaccines against avian coccidiosis
    Shagufta Iqbal, Syed Tanveer, Idrees Mehraj Allaie, Yasmeena Jan, Shahana Tramboo, Nazima Maqbool
    Journal of Microbiological Methods.2025; 238: 107255.     CrossRef
  • Orally delivered Bacillus subtilis expressing chicken NK-2 peptide stabilizes gut microbiota and enhances intestinal health and local immunity in coccidiosis-infected broiler chickens
    Samiru S. Wickramasuriya, Inkyung Park, Youngsub Lee, Luciana M. Richer, Chris Przybyszewski, Cyril G. Gay, Jolieke G. van Oosterwijk, Hyun S. Lillehoj
    Poultry Science.2023; 102(5): 102590.     CrossRef
  • Research progress of the avian coccidiosis vaccine
    Haiming Cai, Nanshan Qi, Juan Li, Minna Lv, Xuhui Lin, Junjing Hu, Jianfei Zhang, Shenquan Liao, Mingfei Sun
    Veterinary Vaccine.2022; 1(1): 100002.     CrossRef
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  • 4 Web of Science
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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

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  • 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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  • 6 Web of Science
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A Novel Anti-Microbial Peptide from Pseudomonas, REDLK Induced Growth Inhibition of Leishmania tarentolae Promastigote In Vitro
Yanhui Yu, Panpan Zhao, Lili Cao, Pengtao Gong, Shuxian Yuan, Xinhua Yao, Yanbing Guo, Hang Dong, Weina Jiang
Korean J Parasitol 2020;58(2):173-179.
Published online April 30, 2020
DOI: https://doi.org/10.3347/kjp.2020.58.2.173
Leishmaniasis is a prevalent cause of death and animal morbidity in underdeveloped countries of endemic area. However, there is few vaccine and effective drugs. Antimicrobial peptides are involved in the innate immune response in many organisms and are being developed as novel drugs against parasitic infections. In the present study, we synthesized a 5-amino acid peptide REDLK, which mutated the C-terminus of Pseudomonas exotoxin, to identify its effect on the Leishmania tarentolae. Promastigotes were incubated with different concentration of REDLK peptide, and the viability of parasite was assessed using MTT and Trypan blue dye. Morphologic damage of Leishmania was analyzed by light and electron microscopy. Cellular apoptosis was observed using the annexin V-FITC/PI apoptosis detection kit, mitochondrial membrane potential assay kit and flow cytometry. Our results showed that Leishmania tarentolae was susceptible to REDLK in a dose-dependent manner, disrupt the surface membrane integrity and caused parasite apoptosis. In our study, we demonstrated the leishmanicidal activity of an antimicrobial peptide REDLK from Pseudomonas aeruginosa against Leishmania tarentolae in vitro and present a foundation for further research of anti-leishmanial drugs.

Citations

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  • Pseudomonas bambusae sp.nov., an Aniline Blue-Decolorizing Bacterium Isolated from Decaying Round Bamboo Culms
    Xiao-Long He, Jia-Yan Wang, Jin-Jia Liang, Cheng-Jing Ren, Xin-Yi Guo, Wen-Jie Ke, Min Wu, Hong-Zheng Liu, Min Jin, Fang-Li Sun, Shuai-Bo Han
    Current Microbiology.2025;[Epub]     CrossRef
  • Therapeutic potential of antimicrobial peptides against pathogenic protozoa
    Corina Lobato Hagemann, Alexandre José Macedo, Tiana Tasca
    Parasitology Research.2024;[Epub]     CrossRef
  • Targeting Leishmania Promastigotes and Amastigotes Forms through Amino Acids and Peptides: A Promising Therapeutic Strategy
    Charmante Registre, Luciana Miranda Silva, Farah Registre, Rodrigo Dian de Oliveira Aguiar Soares, Karina Taciana Santos Rubio, Simone Pinto Carneiro, Orlando David Henrique dos Santos
    ACS Infectious Diseases.2024; 10(8): 2467.     CrossRef
  • Neglected Zoonotic Diseases: Advances in the Development of Cell-Penetrating and Antimicrobial Peptides against Leishmaniosis and Chagas Disease
    Sara M. Robledo, Silvia Pérez-Silanes, Celia Fernández-Rubio, Ana Poveda, Lianet Monzote, Víctor M. González, Paloma Alonso-Collado, Javier Carrión
    Pathogens.2023; 12(7): 939.     CrossRef
  • 6,618 View
  • 105 Download
  • 4 Web of Science
  • Crossref
Evaluation of IgG4 Subclass Antibody Detection by Peptide-Based ELISA for the Diagnosis of Human Paragonimiasis Heterotrema
Pewpan M. Intapan, Oranuch Sanpool, Penchom Janwan, Porntip Laummaunwai, Nimit Morakote, Yoon Kong, Wanchai Maleewong
Korean J Parasitol 2013;51(6):763-766.
Published online December 31, 2013
DOI: https://doi.org/10.3347/kjp.2013.51.6.763

A synthetic peptide was prepared based on the antigenic region of Paragonimus westermani pre-procathepsin L, and its applicability for immunodiagnosis for human paragonimiasis (due to Paragonimus heterotremus) was tested using an ELISA to detect IgG4 antibodies in the sera of patients. Sera from other helminthiases, tuberculosis, and healthy volunteers were used as the references. This peptide-based assay system gave sensitivity, specificity, accuracy, and positive and negative predictive values of 100%, 94.6%, 96.2%, 100%, and 88.9%, respectively. Cross reactivity was frequently seen against the sera of fascioliasis (75%) and hookworm infections (50%). Since differential diagnosis between paragonimiasis and fascioliasis can be easily done by clinical presentation and fascioliasis serology, this cross reaction is not a serious problem. Sera from patients with other parasitoses (0-25%) rarely responded to this synthetic antigen. This synthetic peptide antigen seems to be useful for development of a standardized diagnostic system for paragonimiasis.

Citations

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  • First Report of Isolapotamon sp. as a Potential Intermediate Host of Paragonimus westermani in Davao Oriental, Philippines
    Diadem R. Ricarte, Joshua M. Cambronero, Carmela H. Lorico, Herbert J. Santos, Nestor S. Arce, Aleyla E. de Cadiz
    Parasitologia.2025; 5(4): 67.     CrossRef
  • An immunochromatographic test using whole blood for rapid diagnosis of human paragonimiasis and its diagnostic usefulness
    Patcharaporn Boonroumkaew, Lakkhana Sadaow, Penchom Janwan, Rutchanee Rodpai, Oranuch Sanpool, Tongjit Thanchomnang, Hiroshi Yamasaki, Pewpan M. Intapan, Wanchai Maleewong
    Food and Waterborne Parasitology.2024; 37: e00246.     CrossRef
  • Development of point-of-care testing tool using immunochromatography for rapid diagnosis of human paragonimiasis
    Lakkhana Sadaow, Oranuch Sanpool, Hiroshi Yamasaki, Wanchai Maleewong, Pewpan M. Intapan
    Acta Tropica.2020; 203: 105325.     CrossRef
  • Paragonimus and paragonimiasis in Asia: An update
    Ayako Yoshida, Pham Ngoc Doanh, Haruhiko Maruyama
    Acta Tropica.2019; 199: 105074.     CrossRef
  • A Case of Pulmonary Paragonimiasis with Chronic Abdominal Pain and Erythematous Rash in a 6-year-old Girl
    Ju Young Kim, Min Kyu Park, Yong Ju Lee, Sun Huh, Ky Young Cho
    Pediatric Infection and Vaccine.2018; 25(1): 54.     CrossRef
  • A tool for mass-screening of paragonimiasis: an enzyme-linked immunosorbent assay with urine samples
    Xu Guang Qiu, Fukumi Nakamura-Uchiyama, Yukifumi Nawa, Makoto Itoh
    Tropical Medicine and Health.2016;[Epub]     CrossRef
  • Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani
    Chun-Seob Ahn, Byoung-Kuk Na, Dong-ll Chung, Jeong-Geun Kim, Jin-Taek Kim, Yoon Kong
    Parasitology International.2015; 64(1): 37.     CrossRef
  • North American paragonimiasis: epidemiology and diagnostic strategies
    Peter U Fischer, Gary J Weil
    Expert Review of Anti-infective Therapy.2015; 13(6): 779.     CrossRef
  • 8,912 View
  • 109 Download
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Original Articles
Immunoelectron microscopic localization of partially purified antigens in adult Paragonimus iloktsuenensis
Ok-Ran Lee, Pyung-Rim Chung
Korean J Parasitol 2001;39(2):119-132.
Published online June 30, 2001
DOI: https://doi.org/10.3347/kjp.2001.39.2.119

An immunoelectron microscopy employing immunogold labeling method was performed to detect tissue origin of D1 fraction (D1A) among 5 antigenic protein fractions partially purified by DEAE-anion exchange chromatography from water-soluble crude antigen (PIWA) of adult Paragonimus iloktsuenensis. Immune reactions of adult worm tissues with rabbit serum immunoglobulin immunized with crude antigen (PI-Ig) and D1 antigen (D1-Ig), as well as rat serum immunoglobulin infected with P. iloktsuenensis were observed. D1A showed strong antigenicity in the intestinal epithelium of the worms during the early infection period of 2-4 weeks after infection. The vitellaria also showed stronger antigenicity than the other tissue sites in immune reaction of tissues against all immunoglobulins from 4 to 33 weeks after vitelline development. Therefore, it is suggested that D1A was mainly originated from the intestinal epithelial tissues before the development of vitelline gland of the parasites. Immuno-reactivity of two immunoglobulins (PI-Ig, D1-Ig) was significantly different in intestinal epithelial cytoplasmic protrusions (CP) and intestinal epithelial secretory granules (SG). In the experimental group with D1-Ig, gold particles were labeled significantly in CP than in SG when compared to the PI-Ig group. Thus, the major antigenic materials in D1 antigen having a strong antigenicity in the early infection period was considered to be originated from the intestinal epithelial tissue.

Citations

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  • Nuclear ribosomal transcription units in Asian Paragonimus species (Paragonimidae: Platyhelminthes): genetic characteristics, polymorphism, and implications for intersuperfamilial phylogeny
    Khue Thi Nguyen, Huong Thi Thanh Doan, Linh Thi Khanh Pham, Do Thi Roan, Takeshi Agatsuma, Pham Ngoc Doanh, Thanh Hoa Le
    Parasitology Research.2024;[Epub]     CrossRef
  • Mitogenomic and nuclear ribosomal transcription unit datasets support the synonymy of Paragonimus iloktsuenensis and P. ohirai (Paragonimidae: Platyhelminthes)
    Thanh Hoa Le, Khue Thi Nguyen, Linh Thi Khanh Pham, Huong Thi Thanh Doan, Do Thi Roan, Xuyen Thi Kim Le, Takeshi Agatsuma, David Blair
    Parasitology Research.2023; 122(7): 1531.     CrossRef
  • Paragonimus westermani infection manifesting as a pulmonary cavity and adrenal gland mass: A case report
    Yong Shik Kwon, Hye Won Lee, Hyun Jung Kim
    Journal of Infection and Chemotherapy.2019; 25(3): 200.     CrossRef
  • Ion-exchange protocol to obtain antigenic fractions with potential for serodiagnosis of strongyloidiasis
    H. T. GONZAGA, C. VILA-VERDE, D. S. NUNES, V. S. RIBEIRO, J. P. CUNHA-JÚNIOR, J. M. COSTA-CRUZ
    Parasitology.2013; 140(1): 69.     CrossRef
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Molecular cloning and characterization of an antigenic protein with a repeating region from Clonorchis sinensis
Tae Yun Kim, Shin-Yong Kang, Il-Young Ahn, Seung-Yull Cho, Sung-Jong Hong
Korean J Parasitol 2001;39(1):57-66.
Published online March 31, 2001
DOI: https://doi.org/10.3347/kjp.2001.39.1.57

In the course of immunoscreening of Clonorchis sinensis cDNA library, a cDNA CsRP12 containing a tandem repeat was isolated. The cDNA CsRP12 encodes two putative peptides of open reading frames (ORFs) 1 and 2 (CsRP12-1 and -2). The repetitive region is composed of 15 repeats of 10 amino acids. Of the two putative peptides, CsRP12-1 was proline-rich and found to have homologues in several organisms. Recombinant proteins of the putative peptides were bacterially produced and purified by an affinity chromatography. Recombinant CsRP12-1 protein was recognized by sera of clonorchiasis patients and experimental rabbits, but recombinant CsRP12-2 was not. One of the putative peptide, CsRP12-1, is designated CsPRA, proline-rich antigen of C. sinensis. Both the C-termini of CsRP12-1 and -2 were bacterially produced and analysed to show no antigenicity. Recombinant CsPRA protein showed high sensitivity and specificity. In experimental rabbits, IgG antibodies to CsPRA was produced between 4 and 8 weeks after the infection and decreased thereafter over one year. These results indicate that CsPRA is equivalent to a natural protein and a useful antigenic protein for serodiagnosis of human clonorchiasis.

Citations

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  • A point-of-care testing assay for clonorchiasis using a EuNPs-CsTR1 fluorescent probe-based immunoassay
    Xiaoxiao Ma, Huiyuan Zhang, Yiming Fang, Jing Wang, Xingyang Wang, Chen Li, Xiaolei Liu, Mingyuan Liu, Bin Tang, Yi Liu, Javier Sotillo
    PLOS Neglected Tropical Diseases.2024; 18(4): e0012107.     CrossRef
  • Evaluation of Crude and Recombinant Antigens of Schistosoma japonicum for the Detection of Schistosoma mekongi Human Infection
    Jose Ma. M. Angeles, Atcharaphan Wanlop, Minh-Anh Dang-Trinh, Masashi Kirinoki, Shin-ichiro Kawazu, Aya Yajima
    Diagnostics.2023; 13(2): 184.     CrossRef
  • Combination of Biodata Mining and Computational Modelling in Identification and Characterization of ORF1ab Polyprotein of SARS-CoV-2 Isolated from Oronasopharynx of an Iranian Patient
    Reza Zolfaghari Emameh, Hassan Nosrati, Ramezan Ali Taheri
    Biological Procedures Online.2020;[Epub]     CrossRef
  • Cs1, a Clonorchis sinensis-derived serodiagnostic antigen containing tandem repeats and a signal peptide
    Na Cheng, Xue-Nian Xu, Yan Zhou, Yu-Ting Dong, Yi-Fang Bao, Bin Xu, Wei Hu, Zheng Feng, Maria Elena Bottazzi
    PLOS Neglected Tropical Diseases.2018; 12(8): e0006683.     CrossRef
  • Heat shock proteins 70 and 90 from Clonorchis sinensis induce Th1 response and stimulate antibody production
    Eun Joo Chung, Young-Il Jeong, Myoung-Ro Lee, Yu Jung Kim, Sang-Eun Lee, Shin-Hyeong Cho, Won-Ja Lee, Mi-Yeoun Park, Jung-Won Ju
    Parasites & Vectors.2017;[Epub]     CrossRef
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    Yu-Jung Kim, Won Yoo, Myoung-Ro Lee, Jung-Mi Kang, Byoung-Kuk Na, Shin-Hyeong Cho, Mi-Yeoun Park, Jung-Won Ju
    International Journal of Molecular Sciences.2017; 18(3): 557.     CrossRef
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    Shuqi Wang, Wei Hu
    Frontiers in Microbiology.2014;[Epub]     CrossRef
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    A.M. Martínez-Ibeas, M.J. Perteguer, C. González-Lanza, T. Gárate, M.Y. Manga-González
    Experimental Parasitology.2013; 135(2): 287.     CrossRef
  • Genomics and molecular genetics of Clonorchis sinensis: Current status and perspectives
    Si-Yang Huang, Guang-Hui Zhao, Bao-Quan Fu, Min-Jun Xu, Chun-Ren Wang, Song-Ming Wu, Feng-Cai Zou, Xing-Quan Zhu
    Parasitology International.2012; 61(1): 71.     CrossRef
  • Multiple recombinant antigens of Clonorchis sinensis for serodiagnosis of human clonorchiasis
    Shunyu Li, Jung Guk Shin, Pyo Yun Cho, Tae Im Kim, Sung-Tae Hong, Sung-Jong Hong
    Parasitology Research.2011; 108(5): 1295.     CrossRef
  • Human Antibody Response to Thioredoxin Peroxidase-1 and Tandem Repeat Proteins as Immunodiagnostic Antigen Candidates for Schistosoma japonicum Infection
    Shin-ichiro Kawazu, Masashi Kirinoki, Pilarita Tongol-Rivera, Yasuyuki Goto, Lydia Leonardo, Elena Villacorte, Yuichi Chigusa, Noboru Inoue, Jose Ma. Angeles
    The American Journal of Tropical Medicine and Hygiene.2011; 85(4): 674.     CrossRef
  • Recent Advances in Serodiagnosis for Clonorchiasis
    Tae Im Kim, Sung-Jong Hong
    Hanyang Medical Reviews.2010; 30(3): 232.     CrossRef
  • Functional Genes and Proteins of Clonorchis sinensis
    Tae Im Kim, Byoung-Kuk Na, Sung-Jong Hong
    The Korean Journal of Parasitology.2009; 47(Suppl): S59.     CrossRef
  • Molecular cloning and phylogenetic analysis of Clonorchis sinensis elongation factor-1α
    Tae Yun Kim, Pyo Yun Cho, Jong Won Na, Sung-Jong Hong
    Parasitology Research.2007; 101(6): 1557.     CrossRef
  • Clonorchiasis: an update
    H.-J. Rim
    Journal of Helminthology.2005; 79(3): 269.     CrossRef
  • Immunology and molecular biology of Opisthorchis viverrini infection
    S. Wongratanacheewin, R.W. Sermswan, S. Sirisinha
    Acta Tropica.2003; 88(3): 195.     CrossRef
  • Use of a recombinant Clonorchis sinensis pore-forming peptide, clonorin, for serological diagnosis of clonorchiasis
    Ji-Yun Lee, Tae Yun Kim, Xiao-Xian Gan, Shin-Yong Kang, Sung-Jong Hong
    Parasitology International.2003; 52(2): 175.     CrossRef
  • Analysis of the genes expressed in Clonorchis sinensis adults using the expressed sequence tag approach
    Ji-Sook Lee, Jongweon Lee, Soon-Jung Park, Tai-Soon Yong
    Parasitology Research.2003; 91(4): 283.     CrossRef
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