Parasites, Hosts and Diseases

"antigenic"

Original Articles

Genetic Diversity of Plasmodium vivax in Clinical Isolates from Southern Thailand using PvMSP1, PvMSP3 (PvMSP3α, PvMSP3β) Genes and Eight Microsatellite Markers: Supinya Thanapongpichat, Thunchanok Khammanee, Nongyao Sawangjaroen, Hansuk Buncherd, Aung Win Tun; Korean J Parasitol 2019;57(5):469-479.
Published online October 31, 2019; DOI: https://doi.org/10.3347/kjp.2019.57.5.469

Abstract
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Plasmodium vivax is usually considered morbidity in endemic areas of Asia, Central and South America, and some part of Africa. In Thailand, previous studies indicated the genetic diversity of P. vivax in malaria-endemic regions such as the western part of Thailand bordering with Myanmar. The
objective
of the study is to investigate the genetic diversity of P. vivax circulating in Southern Thailand by using 3 antigenic markers and 8 microsatellite markers. Dried blood spots were collected from Chumphon, Phang Nga, Ranong and, Surat Thani provinces of Thailand. By PCR, 3 distinct sizes of PvMSP3α, 2 sizes of PvMSP3β and 2 sizes of PvMSP1 F2 were detected based on the length of PCR products, respectively. PCR/RFLP analyses of these antigen genes revealed high levels of genetic diversity. The genotyping of 8 microsatellite loci showed high genetic diversity as indicated by high alleles per locus and high expected heterozygosity (H_E). The genotyping markers also showed multiple-clones of infection. Mixed genotypes were detected in 4.8% of PvMSP3α, 29.1% in PvMSP3β and 55.3% of microsatellite markers. These results showed that there was high genetic diversity of P. vivax isolated from Southern Thailand, indicating that the genetic diversity of P. vivax in this region was comparable to those observed other areas of Thailand.

Citations

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Genetic diversity of Plasmodium vivax and Plasmodium falciparum field isolates from Honduras in the malaria elimination phase
Alejandro Zamora, Alejandra Pinto, Denis Escobar, Hugo O. Valdivia, Lesly Chaver, Gloria Ardón, Erick Carranza, Gustavo Fontecha
Current Research in Parasitology & Vector-Borne Diseases.2025; 7: 100230. CrossRef
Genetic Structure of Introduced Plasmodium vivax Malaria Isolates in Greece, 2015–2019
Ioanna Spiliopoulou, Danai Pervanidou, Nikolaos Tegos, Maria Tseroni, Agoritsa Baka, Annita Vakali, Chrisovaladou-Niki Kefaloudi, Vasilios Papavasilopoulos, Anastasia Mpimpa, Eleni Patsoula
Tropical Medicine and Infectious Disease.2024; 9(5): 102. CrossRef
Asymptomatic Malaria Reservoirs in Honduras: A Challenge for Elimination
Sharon Banegas, Denis Escobar, Alejandra Pinto, Marcela Moncada, Gabriela Matamoros, Hugo O. Valdivia, Allan Reyes, Gustavo Fontecha
Pathogens.2024; 13(7): 541. CrossRef
Distinct Allelic Diversity of Plasmodium vivax Merozoite Surface Protein 3-Alpha (PvMSP-3α) Gene in Thailand Using PCR-RFLP
Kanyanan Kritsiriwuthinan, Warunee Ngrenngarmlert, Rapatbhorn Patrapuvich, Supaksajee Phuagthong, Kantima Choosang, Jianbing Mu
Journal of Tropical Medicine.2023; 2023: 1. CrossRef
Genetic Diversity of Plasmodium vivax Field Isolates from the Thai–Myanmar Border during the Period of 2006–2016
Abdifatah Abdullahi Jalei, Wanna Chaijaroenkul, Kesara Na-Bangchang
Tropical Medicine and Infectious Disease.2023; 8(4): 210. CrossRef
Genetic diversity and molecular evolution of Plasmodium vivax Duffy Binding Protein and Merozoite Surface Protein-1 in northwestern Thailand
Parsakorn Tapaopong, Gustavo da Silva, Sittinont Chainarin, Chayanut Suansomjit, Khajohnpong Manopwisedjaroen, Liwang Cui, Cristian Koepfli, Jetsumon Sattabongkot, Wang Nguitragool
Infection, Genetics and Evolution.2023; 113: 105467. CrossRef
Genetic Diversity of Plasmodium vivax Merozoite Surface Protein-3 Alpha and Beta from Diverse Geographic Areas of Thailand
Jiraporn Kuesap, Kanchana Rungsihirunrat, Wanna Chaijaroenkul, Mathirut Mungthin
Japanese Journal of Infectious Diseases.2022; 75(3): 241. CrossRef
Prevalence of Glucose-6-Phosphate Dehydrogenase (G6PD) Deficiency among Malaria Patients in Southern Thailand: 8 Years Retrospective Study
Thunchanok Khammanee, Nongyao Sawangjaroen, Hansuk Buncherd, Aung Win Tun, Supinya Thanapongpichat
The Korean Journal of Parasitology.2022; 60(1): 15. CrossRef
PvMSP-3α and PvMSP-3β genotyping reveals higher genetic diversity in Plasmodium vivax parasites from migrant workers than residents at the China-Myanmar border
Xiaosong Li, Yao Bai, Yanrui Wu, Weilin Zeng, Zheng Xiang, Hui Zhao, Wei Zhao, Xi Chen, Mengxi Duan, Xun Wang, Wenya Zhu, Kemin Sun, Yiman Wu, Yanmei Zhang, Yucheng Qin, Benjamin M. Rosenthal, Liwang Cui, Zhaoqing Yang
Infection, Genetics and Evolution.2022; 106: 105387. CrossRef
Genetic characterization of Plasmodium vivax isolates from Pakistan using circumsporozoite protein (pvcsp) and merozoite surface protein-1 (pvmsp-1) genes as genetic markers
Zainab Bibi, Anam Fatima, Rehana Rani, Ayesha Maqbool, Samea Khan, Shumaila Naz, Shahid Waseem
Malaria Journal.2021;[Epub] CrossRef

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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

Abstract
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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.

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B-cell epitope mapping and characterization of antibody responses to recombinant PvRipr in malaria-exposed individuals
Isabela Ferreira Soares, Cinthia Magalhães Rodolphi, Ana Luiza Carneiro Alencar, Ada da Silva Matos, Rodrigo Nunes Rodrigues-da-Silva, Barbara de Oliveira Baptista, Rodrigo Medeiros Martorano, Hugo Amorim dos Santos de Souza, Evelyn Kety Pratt Riccio, Jen
Frontiers in Immunology.2026;[Epub] CrossRef
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

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Brief Communication

Screening and Identification of Antigenic Proteins from the Hard Tick Dermacentor silvarum (Acari: Ixodidae): Tiantian Zhang, Xuejiao Cui, Jincheng Zhang, Hui Wang, Meng Wu, Hua Zeng, Yuanyuan Cao, Jingze Liu, Yonghong Hu; Korean J Parasitol 2015;53(6):789-793.
Published online December 31, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.6.789

Abstract
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In order to explore tick proteins as potential targets for further developing vaccine against ticks, the total proteins of unfed female Dermacentor silvarum were screened with anti-D. silvarum serum produced from rabbits. The results of western blot showed that 3 antigenic proteins of about 100, 68, and 52 kDa were detected by polyclonal antibodies, which means that they probably have immunogenicity. Then, unfed female tick proteins were separated by 12% SDS-PAGE, and target proteins (100, 68, and 52 kDa) were cut and analyzed by LC-MS/MS, respectively. The comparative results of peptide sequences showed that they might be vitellogenin (Vg), heat shock protein 60 (Hsp60), and fructose-1, 6-bisphosphate aldolase (FBA), respectively. These data will lay the foundation for the further validation of antigenic proteins to prevent infestation and diseases transmitted by D. silvarum.

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Characterization of tick salivary gland and saliva alphagalactome reveals candidate alpha-gal syndrome disease biomarkers
Margarita Villar, Iván Pacheco, Lourdes Mateos-Hernández, Alejandro Cabezas-Cruz, Ala E. Tabor, Manuel Rodríguez-Valle, Albert Mulenga, Katherine M. Kocan, Edmour F. Blouin, José de La Fuente
Expert Review of Proteomics.2021; 18(12): 1099. CrossRef
Extracellular vesicles induce protective immunity against Trichuris muris
R. K. Shears, A. J. Bancroft, G. W. Hughes, R. K. Grencis, D. J. Thornton
Parasite Immunology.2018;[Epub] CrossRef
New approaches and omics tools for mining of vaccine candidates against vector-borne diseases
Josipa Kuleš, Anita Horvatić, Nicolas Guillemin, Asier Galan, Vladimir Mrljak, Mangesh Bhide
Molecular BioSystems.2016; 12(9): 2680. CrossRef

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Original Articles

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

Abstract
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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

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Proteomic Screening of Antigenic Proteins from the Hard Tick, Haemaphysalis longicornis (Acari: Ixodidae): Young-Ha Kim, Mohammad Saiful slam, Myung-Jo You; Korean J Parasitol 2015;53(1):85-93.
Published online February 27, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.1.85

Abstract
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Proteomic tools allow large-scale, high-throughput analyses for the detection, identification, and functional investigation of proteome. For detection of antigens from Haemaphysalis longicornis, 1-dimensional electrophoresis (1-DE) quantitative immunoblotting technique combined with 2-dimensional electrophoresis (2-DE) immunoblotting was used for whole body proteins from unfed and partially fed female ticks. Reactivity bands and 2-DE immunoblotting were performed following 2-DE electrophoresis to identify protein spots. The proteome of the partially fed female had a larger number of lower molecular weight proteins than that of the unfed female tick. The total number of detected spots was 818 for unfed and 670 for partially fed female ticks. The 2-DE immunoblotting identified 10 antigenic spots from unfed females and 8 antigenic spots from partially fed females. Matrix Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF) of relevant spots identified calreticulin, putative secreted WC salivary protein, and a conserved hypothetical protein from the National Center for Biotechnology Information and Swiss Prot protein sequence databases. These findings indicate that most of the whole body components of these ticks are non-immunogenic. The data reported here will provide guidance in the identification of antigenic proteins to prevent infestation and diseases transmitted by H. longicornis.

Citations

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Developmental Proteomics Reveals the Dynamic Expression Profile of Global Proteins of Haemaphysalis longicornis (Parthenogenesis)
Min-Xuan Liu, Xiao-Pei Xu, Fan-Ming Meng, Bing Zhang, Wei-Gang Li, Yuan-Yuan Zhang, Qiao-Ying Zen, Wen-Ge Liu
Life.2025; 15(1): 59. CrossRef
Haemaphysalis longicornis calreticulin is not an effective molecular tool for tick bite diagnosis and disruption of tick infestations
Weiqing Zheng, Haijun Hu, Jiafu Jiang, Xiangrong Sun, Renlong Fu, Huiying Tao, Yangqing Liu, Haiying Chen, Hongmei Ma, Shengen Chen
Veterinary Parasitology.2022; 309: 109775. 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
Catalogue of stage-specific transcripts in Ixodes ricinus and their potential functions during the tick life-cycle
Pavlina Vechtova, Zoltan Fussy, Radim Cegan, Jan Sterba, Jan Erhart, Vladimir Benes, Libor Grubhoffer
Parasites & Vectors.2020;[Epub] CrossRef
Comparative Tandem Mass Tag-Based Quantitative Proteomic Analysis of Tachaea chinensis Isopod During Parasitism
Yingdong Li, Xin Li, Zhibin Han, Weibin Xu, Xiaodong Li, Qijun Chen
Frontiers in Cellular and Infection Microbiology.2019;[Epub] CrossRef
Applying proteomics to tick vaccine development: where are we?
Margarita Villar, Anabel Marina, José de la Fuente
Expert Review of Proteomics.2017; 14(3): 211. CrossRef
Screening and Identification of Antigenic Proteins from the Hard Tick <i>Dermacentor silvarum</i> (Acari: Ixodidae)
Tiantian Zhang, Xuejiao Cui, Jincheng Zhang, Hui Wang, Meng Wu, Hua Zeng, Yuanyuan Cao, Jingze Liu, Yonghong Hu
The Korean Journal of Parasitology.2015; 53(6): 789. CrossRef

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High Expression of Water-Soluble Recombinant Antigenic Domains of Toxoplasma gondii Secretory Organelles: Zhaoshou Yang, Hye-Jin Ahn, Ho-Woo Nam; Korean J Parasitol 2014;52(4):367-376.
Published online August 29, 2014; DOI: https://doi.org/10.3347/kjp.2014.52.4.367

Abstract
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Recombinant antigenic proteins of Toxoplasma gondii are alternative source of antigens which are easily obtainable for serodiagnosis of toxoplasmosis. In this study, highly antigenic secretory organellar proteins, dense granular GRA2 and GRA3, rhoptrial ROP2, and micronemal MIC2, were analyzed by bioinformatics approach to express as water-soluble forms of antigenic domains. The transmembrane region and disorder tendency of 4 secretory proteins were predicted to clone the genes into pGEX-4T-1 vector. Recombinant plasmids were transformed into BL21 (DE3) pLysS E. coli, and GST fusion proteins were expressed with IPTG. As a result, GST fusion proteins with GRA2_25-105, GRA3_39-138, ROP2_324-561, and MIC2_1-284 domains had respectively higher value of IgG avidity. The rGST-GRA2_25-105 and rGST-GRA3_39-138 were soluble, while rGST-ROP2_324-561 and rGST-MIC2_1-284 were not. GRA2_31-71, intrinsically unstructured domain (IUD) of GRA2, was used as a linker to enhance the solubility. The rGST-GRA2_31-71-ROP2_324-561, a chimeric protein, appeared to be soluble. Moreover, rGST-GRA2_31-71-MIC2_1-284 was also soluble and had higher IgG avidity comparing to rGST-MIC2_1-284. These 4 highly expressed and water-soluble recombinant antigenic proteins may be promising candidates to improve the serodiagnosis of toxoplasmosis in addition to the major surface antigen of SAG1.

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Single Cell Expression Systems for the Production of Recombinant Proteins for Immunodiagnosis and Immunoprophylaxis of Toxoplasmosis
Karolina Sołowińska, Lucyna Holec-Gąsior
Microorganisms.2024; 12(8): 1731. CrossRef
A vaccine using Anaplasma marginale subdominant type IV secretion system recombinant proteins was not protective against a virulent challenge
Macarena Sarli, María B. Novoa, Matilde N. Mazzucco, Marcelo L. Signorini, Ignacio E. Echaide, Susana T. de Echaide, María E. Primo, Paulo Lee Ho
PLOS ONE.2020; 15(2): e0229301. CrossRef
Development of a novel fusion protein with Anaplasma marginale and A. centrale MSP5 improved performance of Anaplasma antibody detection by cELISA in infected and vaccinated cattle
María E. Primo, Carolina S. Thompson, Beatriz S. Valentini, Macarena Sarli, María B. Novoa, Atilio J. Mangold, Susana T. de Echaide, Ulrike Gertrud Munderloh
PLOS ONE.2019; 14(1): e0211149. CrossRef
TheToxoplasma gondiidense granule protein TgGRA3 interacts with host Golgi and dysregulates anterograde transport
Maika S. Deffieu, Tchilabalo Dilezitoko Alayi, Christian Slomianny, Stanislas Tomavo
Biology Open.2019;[Epub] CrossRef

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Brief Communication

Identification of Antigenic Proteins in Trichomonas vaginalis: Hye-Yeon Lee, Sujin Hyung, Jong Woong Lee, Juri Kim, Myeong Heon Shin, Jae-Sook Ryu, Soon-Jung Park; Korean J Parasitol 2011;49(1):79-83.
Published online March 18, 2011; DOI: https://doi.org/10.3347/kjp.2011.49.1.79

Abstract
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Trichomoniasis is a sexually transmitted disease due to infection with Trichomonas vaginalis, and it can cause serious consequences for women's health. To study the virulence factors of this pathogen, T. vaginalis surface proteins were investigated using polyclonal antibodies specific to the membrane fractions of T. vaginalis. The T. vaginalis expression library was constructed by cloning the cDNA derived from mRNA of T. vaginalis into a phage λ Uni-ZAP XR vector, and then used for immunoscreening with the anti-membrane proteins of T. vaginalis antibodies. The immunoreactive proteins identified included adhesion protein AP65-1, α-actinin, kinesin-associated protein, teneurin, and 2 independent hypothetical proteins. Immunofluorescence assays showed that AP65-1, one of the identified immunogenic clones, is prevalent in the whole body of T. vaginalis. This study led us to identify T. vaginalis proteins which may stimulate immune responses by human cells.

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Ahmet Efe Köseoğlu, Meltem Kutnu, Buminhan Özgültekin, Gülsüm Deniz Köseoğlu, Sabina Neziri, Bilge İrem Göç, Yusuf Şeflekçi, Nehir Özdemir Özgentürk, Yağmur Ekenoğlu Merdan
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Parasite Immunology.2024;[Epub] CrossRef
Trichomonas vaginalis adhesion protein 65 (TvAP65) modulates parasite pathogenicity by interacting with host cell proteins
Zhenchao Zhang, Xiaoxiao Song, Yangyang Deng, Yuhua Li, Fakun Li, Wanxin Sheng, Xiaowei Tian, Zhenke Yang, Xuefang Mei, Shuai Wang
Acta Tropica.2023; 246: 106996. CrossRef
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Original Article

Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis: Tae-Joon Park, Jung-Mi Kang, Byoung-Kuk Na, Woon-Mok Sohn; Korean J Parasitol 2009;47(4):359-367.
Published online December 1, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.4.359

Abstract
PDF

Paramyosin is a myofibrillar protein present in helminth parasites and plays multifunctional roles in host-parasite interactions. In this study, we identified the gene encoding paramyosin of Clonorchis sinensis (CsPmy) and characterized biochemical and immunological properties of its recombinant protein. CsPmy showed a high level of sequence identity with paramyosin from other helminth parasites. Recombinant CsPmy (rCsPmy) expressed in bacteria had an approximate molecular weight of 100 kDa and bound both human collagen and complement 9. The protein was constitutively expressed in various developmental stages of the parasite. Imunofluorescence analysis revealed that CsPmy was mainly localized in the tegument, subtegumental muscles, and the muscle layer surrounding the intestine of the parasite. The rCsPmy showed high levels of positive reactions (74.6%, 56/75) against sera from patients with clonorchiasis. Immunization of experimental rats with rCsPmy evoked high levels of IgG production. These results collectively suggest that CsPmy is a multifunctional protein that not only contributes to the muscle layer structure but also to non-muscular functions in host-parasite interactions. Successful induction of host IgG production also suggests that CsPmy can be applied as a diagnostic antigen and/or vaccine candidate for clonorchiasis.

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Mapping of the putative epitope domain of Clonorchis sinensis paramyosin (CsPmy) recognized by CsPmy-specific immunoglobulin G in sera of human clonorchiasis
Jung-Mi Kang, Hye-Lim Ju, Jinyoung Lee, Tae Im Kim, Shin-Hyeong Cho, Tong-Soo Kim, Woon-Mok Sohn, Byoung-Kuk Na
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Mini Reviews

Functional Genes and Proteins of Clonorchis sinensis: Tae Im Kim, Byoung-Kuk Na, Sung-Jong Hong; Korean J Parasitol 2009;47(Suppl):S59.
Published online October 27, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.S.S59

Abstract
PDF

During the past several decades, researches on parasite genetics have progressed from biochemical and serodiagnostic studies to protein chemistry, molecular biology, and functional gene studies. Nowadays, bioinformatics, genomics, and proteomics approaches are being applied by Korean parasitology researchers. As for Clonorchis sinensis, investigations have been carried out to identify its functional genes using forward and reverse genetic approaches and to characterize the biochemical and biological properties of its gene products. The authors review the proteins of cloned genes, which include antigenic proteins, physiologic and metabolic enzymes, and the gene expression profile of Clonorchis sinensis.

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Genetic Characteristics of Polymorphic Antigenic Markers among Korean Isolates of Plasmodium vivax: Seung-Young Hwang, So-Hee Kim, Weon-Gyu Kho; Korean J Parasitol 2009;47(Suppl):S51.
Published online October 26, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.S.S51

Abstract
PDF

Plasmodium vivax, a protozoan malaria parasite of humans, represents a major public health concern in the Republic of Korea (= South Korea). However, little is known about the genetic properties and population structures of the P. vivax isolates circulating in South Korea. This article reviews known polymorphic genetic markers in South Korean isolates of P. vivax and briefly summarizes the current issues surrounding the gene and population structures of this parasite. The critical genetic characteristics of major antigens of the parasite, such as circumsporozoite protein (CSP), merozoite surface protein 1 (MSP-1) and MSP-3, Duffy binding protein (DBP), apical membrane antigen 1 (AMA-1), and GAM-1, are also discussed.

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Genetic Diversity of Plasmodium vivax Causing Epidemic Malaria in the Republic of Korea
Young Yil Bahk, Jeonga Kim, Seong Kyu Ahn, Byoung-Kuk Na, Jong-Yil Chai, Tong-Soo Kim
The Korean Journal of Parasitology.2018; 56(6): 545. CrossRef
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PLoS Neglected Tropical Diseases.2012; 6(4): e1592. CrossRef
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Malaria Journal.2010;[Epub] CrossRef

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Brief Communication

Ultrastructural Localization of Cryptosporidium parvum Antigen Using Human Patients Sera: Jong-Gyu Lee, Eun-Taek Han, Woo-Yoon Park, Jae-Ran Yu; Korean J Parasitol 2009;47(2):171-174.
Published online May 27, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.2.171

Abstract
PDF

The antigen location of Cryptosporidium parvum, which stimulates antibody formation in humans and animals, was investigated using infected human sera. Immuno-electron microscopy revealed that antigenicity-inducing humoral immunity was located at various developmental stages of parasites, including asexual, sexual stages, and oocysts. The amount of antigen-stimulating IgG antibodies was particularly high on the oocyst wall. The sporozoite surface was shown to give stimulation on IgG and IgM antibody formation. Trophozoites implicated the lowest antigenicity to humoral immunity, both IgG and IgM, by showing the least amount of gold labeling. Immunogold labeling also provided clues that antigens were presented to the host-cell cytoplasm via feeder organelles and host-parasite junctions.

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Cryptostatin, a chagasin-family cysteine protease inhibitor ofCryptosporidium parvum
J.-M. KANG, H.-L. JU, J.-R. YU, W.-M. SOHN, B.-K. NA
Parasitology.2012; 139(8): 1029. CrossRef

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Original Articles

Antibody Responses to Cryptosporidium Antigen in HIV-positive Patients in the Republic of Korea: Sang-Mee Guk, Jong-Yil Chai, Yung-Oh Shin, Min Seo; Korean J Parasitol 2008;46(2):71-75.
Published online June 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.2.71

Abstract
PDF

The diagnosis of cryptosporidiosis has been carried out using coprologic techniques in the Republic of Korea. However, antibody responses to Cryptosporidium have rarely been studied. Serum antibodies from HIV-positive/oocyst-positive Korean patients recognized significantly 31 and 27 kDa antigens, and HIV-negative/oocyst-positive individuals clearly reacted to 15/17 kDa antigens. Compared with oocyst-positive cases, 18.7% and 75.8% of sera from HIV-positive patients reacted to 31 and 27 kDa antigens. Only 11.1% of HIV-negative individuals reacted to 15/17 kDa. Based on these findings, serum antibody responses were different between HIV-positive and HIV-negative individuals infected with Cryptosporidium, and it is suggested that HIV-positive patients are more frequently exposed to C. parvum compared to HIV-negative individuals.

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Review of Successful Control of Parasitic Infections in Korea
Sung-Tae Hong, Tai-Soon Yong
Infection & Chemotherapy.2020; 52(3): 427. CrossRef
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Edward T. Ryan, Elena Naumova, Mohammad M. Karim, Anoli J. Borad, Sitara Swarna Rao Ajjampur, Honorine D. Ward, Gagandeep Kang, Joy Moy, Geneve M. Allison, Stephen B. Calderwood, Sabeena Ahmed, Patricia L. Hibberd, Anne V. Kane, Wasif A. Khan, David Wang
The American Journal of Tropical Medicine and Hygiene.2012; 86(2): 214. CrossRef

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Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation: Young-Bae Chung, Yoon Kong, Hyun-Jong Yang; Korean J Parasitol 2004;42(2):57-60.
Published online June 20, 2004; DOI: https://doi.org/10.3347/kjp.2004.42.2.57

Abstract
PDF

A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electrophoretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-glycosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.

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Characterization of the carbohydrate components of Taenia solium oncosphere proteins and their role in the antigenicity
Yanina Arana, Manuela Verastegui, Iskra Tuero, Louis Grandjean, Hector H. Garcia, Robert H. Gilman
Parasitology Research.2013; 112(10): 3569. CrossRef

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Molecular cloning of ribosomal P protein in Toxoplasma gondii and the availability to detect antibody against recombinant protein in toxoplasmosis patients: Hye-Jin Ahn, Sera Kim, Ho-Woo Nam; Korean J Parasitol 2003;41(2):89-96.
Published online June 20, 2003; DOI: https://doi.org/10.3347/kjp.2003.41.2.89

Abstract
PDF

Among the panel of monoclonal antibodies (mAb) against Toxoplasma gondii, mAb of Tg621 (Tg621) clone blotted 38 kDa protein which localized in the cytoplasm of tachyzoites by immunofluorescence microscopy. The protein was not released into the parasitophorous vacuole during or after invasion. The cDNA fragment encoding the protein was obtained by screening a T. gondii cDNA expression library with Tg621. The full length cDNA sequence was completed with 5'-RACE as 1,592 bp, which contained open reading frame of 942 bp. The deduced amino acid sequence of Tg621 consisted of a polypeptide of 313 amino acids, with significant homology to ribosomal P proteins (RPP) of other organisms especially high to those of apicomplexan species. The expressed and purified TgRPP was assayed in western blot with the sera of toxoplasmosis patients and normal sera, which resulted in the 74.0% of positive reactions in toxoplasmosis patients whereas 8.3% in normal group. Therefore, the antibody formation against TgRPP in toxoplasmosis patients was regarded as specific for T. gondii infection and suggested a potential autoantibody.

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Infection and Immunity.2004; 72(9): 5515. CrossRef

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Determination of antigenic domain in GST fused major surface protein (Nc-p43) of Neospora caninum: Eui-Sun Son, Hye-Jin Ahn, Jae-Hoon Kim, Dae-Yong Kim, Ho-Woo Nam; Korean J Parasitol 2001;39(3):241-246.
Published online September 30, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.3.241

Abstract
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The antigenic domain of the major surface protein (Nc-p43) of Neospora caninum was examined by polymerase chain reaction of its gene fragments and recombinant expression as GST fusion proteins. The fragments of Nc-p43 were as follow: a total open reading frame (OFR), T; OFR without signal sequence and C-terminal hydrophobic sequence, S; N-terminal 2/3 parts of S, A; C-terminal 2/3 parts, P; N-terminal 1/3 part, X; middle 1/3 part, Y; and C-terminal 1/3 part, Z, respectively. The DNA fragments were cloned into pGEX-4T vector. Recombinant plasmids transformed into Escherichia coli of BL21 pLysS (DE3) strain were induced to express GST or GST fused fragments of Nc-p43 such as 69 kDa protein for T, 66 kDa for S, 52 kDa for A, 53 kDa for P, and 40 kDa proteins for X, Y, and Z, respectively in SDS-PAGE. The Nc-p43 fragments of T, S, and P reacted with a bovine serum of neosporosis while those of A, X, Y, and Z together with GST did not in the western blot. These findings suggest that the antigenic domain of Nc-p43 of N. caninum may be localized in the C-terminal 2/3 parts. Together with A19 clone in SAG1 of Toxoplasma gondii (Nam et al., 1996), the P fragment of Nc-p43 could be used as efficient antigens to diagnose and differentiate those infections with both species.

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ELISA detection of IgG antibody against a recombinant major surface antigen (Nc-p43) fragment of Neospora caninum in bovine sera
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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

Abstract
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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.

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Antibody reaction of human anti-Toxoplasma gondii positive and negative sera with Neospora caninum antigens: Ho-Woo Nam, Seung-Won Kang, Won-Young Choi; Korean J Parasitol 1998;36(4):269-275.
Published online December 20, 1998; DOI: https://doi.org/10.3347/kjp.1998.36.4.269

Abstract
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Anti-Neospora caninum antibody was detected in anti-Toxoplasma gondii positive and negative human sera by ELISA, western blot and immunofluorescence assay (IFA). Twelve cases out of 172 (6.7%) Toxoplasma-positive sera cross-reacted with both T. gondii and N. caninum antigens, and one out of 110 Toxoplasma-negative sera reacted with N. caninum antigen by ELISA. By western blot, all 12 sera reacted with T. gondii antigens with various banding patterns but specifically at 30 kDa (SAG1) and 22 kDa (SAG2) bands. With N. caninum antigen, the number of reactive bands was reduced, however a 43 kDa band reacted in three cases in Toxoplasma-positive sera in addition to one in Toxoplasma-negative control sera. All sera of the Toxoplasma-positive group labeled surface membrane of T. gondii, but reacted differently with N. caninum. Fluorescence was detected in surface membrane, subcellular organelles, or both in N. caninum. And one case in the Toxoplasma-negative group also reacted with N. caninum strongly in subcellular organelles. This suggested that the antibody against N. caninum may be present in human sera although the positive rate was very low in this study. The possibility of human infection with N. caninum remains to be evaluated further.

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