Parasites, Hosts and Diseases

"antigenicity"

Original Articles

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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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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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.

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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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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
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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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Among-population proteomic differences in Schistocephalus solidus based on excretory/secretory and total body protein predictions
Anni Wang, Daniel I. Bolnick
Parasites & Vectors.2025;[Epub] CrossRef
What about the Cytoskeletal and Related Proteins of Tapeworms in the Host’s Immune Response? An Integrative Overview
Diana G. Ríos-Valencia, Javier Ambrosio, Rocío Tirado-Mendoza, Julio César Carrero, Juan Pedro Laclette
Pathogens.2023; 12(6): 840. CrossRef
Current status of Clonorchis sinensis and clonorchiasis in Korea: epidemiological perspectives integrating the data from human and intermediate hosts
Won Gi Yoo, Woon-Mok Sohn, Byoung-Kuk Na
Parasitology.2022; 149(10): 1296. CrossRef
Mapping of the Complement C9 Binding Region on Clonorchis sinensis Paramyosin
Jung-Mi Kang, Hương Giang Lê, Tuấn Cường Võ, Won Gi Yoo, Woon-Mok Sohn, Byoung-Kuk Na
The Korean Journal of Parasitology.2022; 60(4): 255. CrossRef
Characterization of paramyosin protein structure and gene expression during myogenesis in Pacific oyster (Crassostrea gigas)
Huijuan Li, Qi Li, Hong Yu, Shaojun Du
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology.2021; 255: 110594. CrossRef
Clonorchis sinensis and clonorchiasis
Byoung-Kuk Na, Jhang Ho Pak, Sung-Jong Hong
Acta Tropica.2020; 203: 105309. CrossRef
Proteomic and Bioinformatic Investigations of Heat-Treated Anisakis simplex Third-Stage Larvae
Maciej Kochanowski, Mirosław Różycki, Joanna Dąbrowska, Aneta Bełcik, Jacek Karamon, Jacek Sroka, Tomasz Cencek
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Bacillus subtilis spore with surface display of paramyosin from Clonorchis sinensis potentializes a promising oral vaccine candidate
Hengchang Sun, Zhipeng Lin, Lu Zhao, Tingjin Chen, Mei Shang, Hongye Jiang, Zeli Tang, Xinyi Zhou, Mengchen Shi, Lina Zhou, Pengli Ren, Honglin Qu, Jinsi Lin, Xuerong Li, Jin Xu, Yan Huang, Xinbing Yu
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Infection by the Helminth Parasite Fasciola hepatica Requires Rapid Regulation of Metabolic, Virulence, and Invasive Factors to Adjust to Its Mammalian Host
Krystyna Cwiklinski, Heather Jewhurst, Paul McVeigh, Tara Barbour, Aaron G. Maule, Jose Tort, Sandra M. O'Neill, Mark W. Robinson, Sheila Donnelly, John P. Dalton
Molecular & Cellular Proteomics.2018; 17(4): 792. CrossRef
Paramyosin of canine Onchocerca lupi: usefulness for the diagnosis of a neglected zoonotic disease
Bronwyn Campbell, Helder Cortes, Giada Annoscia, Alessio Giannelli, Antonio Parisi, Maria Stefania Latrofa, Filipe Dantas-Torres, Luís Cardoso, Domenico Otranto
Parasites & Vectors.2016;[Epub] CrossRef
Proteomic analysis of the excretory/secretory products and antigenic proteins of Echinococcus granulosus adult worms from infected dogs
Ying Wang, Di Xiao, Yujuan Shen, Xiuming Han, Fei Zhao, Xiaohong Li, Weiping Wu, Hejun Zhou, Jianzhong Zhang, Jianping Cao
BMC Veterinary Research.2015;[Epub] CrossRef
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
Molecular and Biochemical Parasitology.2015; 201(1): 66. CrossRef
Trichinella spiralis Paramyosin Binds Human Complement C1q and Inhibits Classical Complement Activation
Ran Sun, Xi Zhao, Zixia Wang, Jing Yang, Limei Zhao, Bin Zhan, Xinping Zhu, Elizabeth Angelica Leme Martins
PLOS Neglected Tropical Diseases.2015; 9(12): e0004310. CrossRef
The identification of antigenic proteins: 14-3-3 protein and propionyl-CoA carboxylase in Clonorchis sinensis
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Molecular identification and characterization of leucine aminopeptidase 2, an excretory-secretory product of Clonorchis sinensis
Chuanhuan Deng, Jiufeng Sun, Xuerong Li, Lexun Wang, Xuchu Hu, Xiaoyun Wang, Wenjun Chen, Xiaoli Lv, Chi Liang, Wenfang Li, Yan Huang, Ran Li, Zhongdao Wu, Xinbing Yu, Jin Xu
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Synthetic peptide-targeted selection of phage display mimotopes highlights immunogenic features of α-helical vs non-helical epitopes of Taenia solium paramyosin: Implications for parasite- and host-protective roles of the protein
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Peptides.2012; 34(1): 232. CrossRef
Identification and Characterization of Paramyosin from Cyst Wall of Metacercariae Implicated Protective Efficacy against Clonorchis sinensis Infection
Xiaoyun Wang, Wenjun Chen, Xiaoli Lv, Yanli Tian, Jingtao Men, Xifeng Zhang, Huali Lei, Chenhui Zhou, Fangli Lu, Chi Liang, Xuchu Hu, Jin Xu, Zhongdao Wu, Xuerong Li, Xinbing Yu, Erika Martins Braga
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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
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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

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
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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
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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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Expression and characterization of Pen b 26 allergen of Penicillium brevicompactum in Escherichia coli
M. Serdal Sevinc, Veena Kumar, Makonnen Abebe, Susantha Mohottalage, Premkumari Kumarathasan, Renaud Vincent, Hari M. Vijay
Protein Expression and Purification.2009; 65(1): 8. CrossRef
Identification of ribosomal phosphoprotein P0 of Neospora caninum as a potential common vaccine candidate for the control of both neosporosis and toxoplasmosis
Houshuang Zhang, Eung-goo Lee, Min Liao, Muller K.A. Compaore, Guohong Zhang, Osamu Kawase, Kozo Fujisaki, Chihiro Sugimoto, Yoshifumi Nishikawa, Xuenan Xuan
Molecular and Biochemical Parasitology.2007; 153(2): 141. CrossRef
Enzyme-catalyzed amplified immunoassay for the detection of Toxoplasma gondii-specific IgG using Faradaic impedance spectroscopy, CV and QCM
Yanjun Ding, Hua Wang, Guoli Shen, Ruqin Yu
Analytical and Bioanalytical Chemistry.2005; 382(7): 1491. CrossRef
Host cell binding of GRA10, a novel, constitutively secreted dense granular protein from Toxoplasma gondii
Hye-Jin Ahn, Sehra Kim, Ho-Woo Nam
Biochemical and Biophysical Research Communications.2005; 331(2): 614. CrossRef
The P Domain of the P0 Protein ofPlasmodium falciparumProtects against Challenge with Malaria Parasites
K. Rajeshwari, Kalpesh Patel, Savithri Nambeesan, Monika Mehta, Alfica Sehgal, Tirtha Chakraborty, Shobhona Sharma
Infection and Immunity.2004; 72(9): 5515. CrossRef

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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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