Parasites, Hosts and Diseases

"epitope"

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.

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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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Multi-Epitope Fusion Protein Eg mefAg-1 as a Serodiagnostic Candidate for Cystic Echinococcosis in Sheep: Liu Tianli, Wang Xifeng, Tian Zhenzhong, Wang Lixia, Zhang Xingxing, Qiao Jun, Meng Qingling, Gong Shasha, Chen Ying, Cai Xuepeng; Korean J Parasitol 2019;57(1):61-67.
Published online February 26, 2019; DOI: https://doi.org/10.3347/kjp.2019.57.1.61

Abstract
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Cystic echinococcosis (CE) in sheep is a hazardous zoonotic parasitic disease that is caused by Echinococcus granulosus (Eg). At present, serological test is an important diagnostic method for Eg infection in domestic animals. Here, a fusion protein Eg mefAg-1 harboring 8 dominant B-cell epitopes of Eg such as antigen B, tetraspanin 1, tetraspanin 6, reticulon and Eg95 was produced in E. coli and evaluated for CE in sheep by indirect ELISA. Eg mefAg-1 showed in ELISA a high sensitivity (93.41%) and specificity (99.31%), with a coincidence rate of 97.02%. Overall, it is suggested that the Eg mefAg-1 could be a potential antigen candidate for CE serodiagnosis in sheep.

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Rapid and non‐invasive detection of cystic echinococcosis in sheep based on serum fluorescence spectrum combined with machine learning algorithms
Shengke Xu, Wubulitalifu Dawuti, Maierhaba Maimaitiaili, Jingrui Dou, Malike Aizezi, Kalibixiati Aimulajiang, Xiaoyi Lü, Guodong Lü
Journal of Biophotonics.2024;[Epub] CrossRef
Recombinant multiepitope proteins expressed in Escherichia coli cells and their potential for immunodiagnosis
Ana Alice Maia Gonçalves, Anna Julia Ribeiro, Carlos Ananias Aparecido Resende, Carolina Alves Petit Couto, Isadora Braga Gandra, Isabelle Caroline dos Santos Barcelos, Jonatas Oliveira da Silva, Juliana Martins Machado, Kamila Alves Silva, Líria Souza Si
Microbial Cell Factories.2024;[Epub] CrossRef
Expression and serodiagnostic efficacy of a novel echinococcosis-specific recombinant fusion antigen rAgB8/1-Em18-Eg95
Yang Xianwei, Wang Tao, Chen Yin, Wang Wentao
Parasitology.2024; 151(13): 1458. CrossRef
Rapid and accurate screening of cystic echinococcosis in sheep based on serum Fourier‐transform infrared spectroscopy combined with machine learning algorithms
Wubulitalifu Dawuti, Jingrui Dou, Xiangxiang Zheng, Xiaoyi Lü, Hui Zhao, Lingfei Yang, Renyong Lin, Guodong Lü
Journal of Biophotonics.2023;[Epub] CrossRef
Evaluation of a novel Echinococcus granulosus recombinant fusion B-EpC1 antigen for the diagnosis of human cystic echinococcosis using indirect ELISA in comparison with a commercial diagnostic ELISA kit
Enayat Darabi, Elahe Motevaseli, Mehdi Mohebali, Mohammad Bagher Rokni, Mohammad Reza Khorramizadeh, Farzaneh Zahabiun, Soudabeh Heidari, Eshrat Beigom Kia
Experimental Parasitology.2022; 240: 108339. CrossRef
Detection of Echinococcus granulosus sensu lato infection by using extracts derived from a protoscoleces G1 cell line
Andrea Maglioco, Jorge Gentile, Melisa S. Barbery Venturi, Oscar Jensen, Claudia Hernández, María Laura Gertiser, Verónica Poggio, Gabriela Canziani, Alicia Graciela Fuchs
Parasite Immunology.2019;[Epub] CrossRef

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Original Articles

Identifying Novel B Cell Epitopes within Toxoplasma gondii GRA6: Yanhua Wang, Guangxiang Wang, Jian Ping Cai; Korean J Parasitol 2016;54(4):431-437.
Published online August 31, 2016; DOI: https://doi.org/10.3347/kjp.2016.54.4.431

Abstract
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The study of antigenic epitopes from Toxoplasma gondii has not only enhanced our understanding of the structure and function of antigens, the reactions between antigens and antibodies, and many other aspects of immunology, but it also plays a significant role in the development of new diagnostic reagents and vaccines. In the present study, T. gondii GRA6 epitopes were identified using bioinformatics tools and a synthetic peptide technique. The potential B cell epitopes of GRA6 predicted by bioinformatics tools concentrated upon 3 regions of GRA6, 1-20 aa, 44-103 aa, and 172-221 aa. Ten shorter peptides from the 3 regions were synthesized and assessed by ELISA using pig sera from different time points after infection. Three of the 10 peptides (amino acids 44-63, 172-191, and 192-211) tested were recognized by all sera and determined to be immunodominant B-cell epitopes of GRA6. The results indicated that we precisely and accurately located the T. gondii GRA6 epitopes using pig sera collected at different time points after infection. The identified epitopes may be very useful for further studies of epitope-based vaccines and diagnostic reagents.

Citations

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A Structural In Silico Analysis of Novel Epitopes from Toxoplasma gondii Proteins for the Serodiagnosis of Toxoplasmosis
Angelis del Valle Benitez Betancourt, Tamires Lopes Silva, Débora Karolla de Freitas Oliveira, Nilson Nicolau-Junior, João Luis Garcia, Ricardo Toshio Fujiwara, Tiago Wilson Patriarca Mineo, José Roberto Mineo
International Journal of Molecular Sciences.2025; 26(10): 4689. CrossRef
Harnessing antigenic proteins of Toxoplasma gondii for efficient diagnosis: a study of promising candidates
Saumya Srivastava, Anil Kumar Gupta, Amit Singh, Sudip Kumar Datta, Sarman Singh
Journal of Parasitic Diseases.2025; 49(4): 897. CrossRef
Letter to the editor of Heliyon re: Bioinformatics-based prediction and screening of immunogenic epitopes of Toxoplasma gondii rhoptry proteins 7, 21 and 22 as candidate vaccine target
Fariha Ayub, Haroon Ahmed, Tehreem Sohail, Khurram Shahzad, Figen Celik, Xu Wang, Sami Simsek, Jianping Cao
Heliyon.2024; 10(14): e32221. CrossRef
Trend in serological and molecular diagnostic methods for Toxoplasma gondii infection
Min-ju Kim, Soeun J. Park, Hyunwoo Park
European Journal of Medical Research.2024;[Epub] CrossRef
Design of a polytopic construct of LACK, TSA and GP63 proteins for the diagnosis of cutaneous leishmaniasis: An in silico strategy
Zahra Arab-Mazar, Mehdi Mohebali, Mohammad Mehdi Ranjbar, Seyyed Javad Seyyed Tabaei, Amirreza Javadi Mamaghani, Niloofar Taghipour
Journal of Asia-Pacific Entomology.2022; 25(4): 101982. CrossRef
First identification of Nocardia seriolaeGapA adhesion function and its three B‐cell epitopes with cell‐binding activity
Jiajing Guo, Xiaozhen Yue, Jiaojiao Chang, Zhenyuan Zhang, Jinnian Li, Xuelan Liu
Journal of Fish Diseases.2022; 45(12): 1845. CrossRef
Strongyloides stercoralis proteome: A reverse approach to the identification of potential immunogenic candidates
Maritza Fernandez Culma
Microbial Pathogenesis.2021; 152: 104545. CrossRef
A peptide originated from Toxoplasma gondii microneme 8 displaying serological evidence to differentiate recent from chronic human infection
Silas Silva Santana, Vinícius Fernandes Paiva, Fernando Reis Carvalho, Heber Leão Silva Barros, Tamires Lopes Silva, Patrício Silva Cardoso Barros, Ana Cláudia Arantes Marquez Pajuaba, Geisa Baptista Barros, Reynaldo Dietze, Tiago Wilson Patriarca Mineo,
Parasitology International.2021; 84: 102394. CrossRef
Design and expression of polytopic construct of cathepsin-L1, SAP-2 and FhTP16.5 proteins of Fasciola hepatica
S. Aghamolaei, B. Kazemi, M. Bandehpour, M.M. Ranjbar, S. Rouhani, A. Javadi Mamaghani, S.J.S. Tabaei
Journal of Helminthology.2020;[Epub] CrossRef
Structural and immunological characterization of a new nucleotidyltransferase-like antigen from Paracoccidioides brasiliensis
Juliana B. Coitinho, Mariana A.F. Costa, Eliza M. Melo, Elis A. Morais, Lorena G.A. de Andrade, Aline M. da Rocha, Mariana T.Q. de Magalhães, Denize C. Favaro, Lucas Bleicher, Enio R.P. Pedroso, Alfredo M. Goes, Ronaldo A.P. Nagem
Molecular Immunology.2019; 112: 151. CrossRef
Candidate antigenic epitopes for vaccination and diagnosis strategies of Toxoplasma gondii infection: A review
Amirreza Javadi Mamaghani, Anwar Fathollahi, Adel Spotin, Mohammad mehdi Ranjbar, Meisam Barati, Somayeh Aghamolaie, Maryam Karimi, Niloofar Taghipour, Mohammad Ashrafi, Seyyed Javad Seyyed Tabaei
Microbial Pathogenesis.2019; 137: 103788. CrossRef
Identification of universal diagnostic peptide candidates for neglected tropical diseases caused by cestodes through the integration of multi-genome-wide analyses and immunoinformatic predictions
Sebastián Miles, Marco Navatta, Sylvia Dematteis, Gustavo Mourglia-Ettlin
Infection, Genetics and Evolution.2017; 54: 338. CrossRef

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Screening and Molecular Cloning of a Protective Antigen from the Midgut of Haemaphysalis longicornis: Yonghong Hu, Jincheng Zhang, Shujie Yang, Hui Wang, Hua Zeng, Tiantian Zhang, Jingze Liu; Korean J Parasitol 2013;51(3):327-334.
Published online June 30, 2013; DOI: https://doi.org/10.3347/kjp.2013.51.3.327

Abstract
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Vaccination is considered a promising alternative for controlling tick infestations. Haemaphysalis longicornis midgut proteins separated by SDS-PAGE and transferred to polyvinylidene difluoride (PVDF) membrane were screened for protective value against bites. The western blot demonstrated the immunogenicity of 92 kDa protein (P92). The analysis of the P92 amino acid sequence by LC-MS/MS indicated that it was a H. longicornis paramyosin (Hl-Pmy). The full lenghth cDNA of Hl-Pmy was obtained by rapid amplification of cDNA ends (RACE) which consisted of 2,783 bp with a 161 bp 3' untranslated region. Sequence alignment of tick paramyosin (Pmy) showed that Hl-Pmy shared a high level of conservation among ticks. Comparison with the protective epitope sequence of other invertebrate Pmy, it was calculated that the protective epitope of Hl-Pmy was a peptide (LEEAEGSSETVVEMNKKRDTE) named LEE, which was close to the N-terminal of Hl-Pmy protein. The secondary structure analysis suggested that LEE had non-helical segments within an α-helical structure. These results provide the basis for developing a vaccine against biting H. longicornis ticks.

Citations

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The current strategies and underlying mechanisms in the control of the vector tick, Haemaphysalis longicornis: Implications for future integrated management
Chuks F. Nwanade, Min Wang, Sisi Li, Zhijun Yu, Jingze Liu
Ticks and Tick-borne Diseases.2022; 13(2): 101905. CrossRef
Evaluation on two types of paramyosin vaccines for the control of Haemaphysalis longicornis infestations in rabbits
Pin-Xing Wu, Xue-Jiao Cui, Mi-Xue Cao, Li-Hong Lv, Hong-Meng Dong, Shu-Wen Xiao, Jing-Ze Liu, Yong-Hong Hu
Parasites & Vectors.2021;[Epub] CrossRef
Morphology and ultrastructure changes of Haemaphysalis longicornis Neumann (Acari: Ixodidae) female adult ticks at different developmental stages
Fang Wang, Duo Wang, Chao-Zhong Jiang, Na Liang, Yong-Hong Hu, Jing-Ze Liu
International Journal of Acarology.2017; 43(4): 308. CrossRef
Evaluation of immune protection induced by DNA vaccines from Haemaphysalis longicornis paramyosin in rabbits
Tian-Tian Zhang, Jin-Cheng Zhang, Xue-Jiao Cui, Jing-Jing Zheng, Ru Li, Fang Wang, Jing-Ze Liu, Yong-Hong Hu
Parasites & Vectors.2017;[Epub] 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
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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IgE Binding Reactivity of Peptide Fragments of Bla g 4, a Major German Cockroach Allergen: Kwang Hyun Shin, Kyoung Yong Jeong, Chein-Soo Hong, Tai-Soon Yong; Korean J Parasitol 2009;47(1):31-36.
Published online March 12, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.1.31

Abstract
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Cockroaches have been recognized as a major cause of asthma. Bla g 4 is one of the most important German cockroach allergens. The aim of this study is to investigate IgE reactivity to the recombinant Bla g 4 (rBla g 4) in the sera of allergic patients and identify linear IgE binding epitope. For protein expression, full-length Bla g 4 (EF202172) was divided into 5 overlapping peptide fragments (E1: aa 1-100, E2: aa 34-77, E3: aa 74-117, E4: aa 114-156, and E5: aa 153-182). The full-length and 5 peptide fragments of Bla g 4 was generated by PCR and over-expressed in E. coli BL21 (DE3). The IgE binding reactivities of the full-length and peptide fragments were measured by ELISA using 32 serum samples of cockroach allergy. The sera of 8 patients (25%) reacted with rBla g 4. Four sera (100%) showed IgE-binding reactivity to full-length and peptide fragment 4, and 2 sera (50%) reacted with peptide fragment 2. One (20%) serum reacted with peptide fragment 3. The results of ELISA using overlapping recombinant fragments indicated that the epitope region was located at amino acid sequences 34-73 and 78-113, and major IgE epitope of Bla g 4 was located at amino acid sequences 118-152 of C-terminal. B-cell epitope analysis of German cockroach allergen Bla g 4 could contribute to the strategic development of more specific and potentially efficacious immunotherapy.

Citations

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Variability in German Cockroach Extract Composition Greatly Impacts T Cell Potency in Cockroach-Allergic Donors
Giovanni Birrueta, April Frazier, Anna Pomés, Jill Glesner, Stephanie Filep, Coby Schal, Kyoung Yong Jeong, Curtis McMurtrey, Thomas Vander Schans, William H. Hildebrand, Paula Busse, Avraham Beigelman, Leonard B. Bacharier, Bjoern Peters, Alessandro Sett
Frontiers in Immunology.2019;[Epub] CrossRef
Insect (food) allergy and allergens
Steffie de Gier, Kitty Verhoeckx
Molecular Immunology.2018; 100: 82. CrossRef
Cockroach allergen exposure and risk of asthma
D. C. Do, Y. Zhao, P. Gao
Allergy.2016; 71(4): 463. CrossRef
IgE-Binding Epitope Mapping and Tissue Localization of the Major American Cockroach Allergen Per a 2
Mey-Fann Lee, Chia-Wei Chang, Pei-Pong Song, Guang-Yuh Hwang, Shyh-Jye Lin, Yi-Hsing Chen
Allergy, Asthma & Immunology Research.2015; 7(4): 376. CrossRef
Different Bla‐g T cell antigens dominate responses in asthma versus rhinitis subjects
M. B. C. Dillon, V. Schulten, C. Oseroff, S. Paul, L. M. Dullanty, A. Frazier, X. Belles, M.‐D. Piulachs, C. Visness, L. Bacharier, G. R. Bloomberg, P. Busse, J. Sidney, B. Peters, A. Sette
Clinical & Experimental Allergy.2015; 45(12): 1856. CrossRef
The major cockroach allergen Bla g 4 binds tyramine and octopamine
Lesa R. Offermann, Siew Leong Chan, Tomasz Osinski, Yih Wan Tan, Fook Tim Chew, J. Sivaraman, Yu-Keung Mok, Wladek Minor, Maksymilian Chruszcz
Molecular Immunology.2014; 60(1): 86. CrossRef
Environmental assessment and exposure reduction of cockroaches: A practice parameter
Jay Portnoy, Ginger L. Chew, Wanda Phipatanakul, P. Brock Williams, Carl Grimes, Kevin Kennedy, Elizabeth C. Matsui, J. David Miller, David Bernstein, Joann Blessing-Moore, Linda Cox, David Khan, David Lang, Richard Nicklas, John Oppenheimer, Christopher
Journal of Allergy and Clinical Immunology.2013; 132(4): 802. CrossRef
Identification of Novel Allergenic Components from German Cockroach Fecal Extract by a Proteomic Approach
Kyoung Yong Jeong, Chung-ryul Kim, Jina Park, In-Soo Han, Jung-Won Park, Tai-Soon Yong
International Archives of Allergy and Immunology.2013; 161(4): 315. CrossRef
The Cockroach and Allergic Diseases
Myung Hyun Sohn, Kyu-Earn Kim
Allergy, Asthma & Immunology Research.2012; 4(5): 264. CrossRef
Der-p2 (Dermatophagoides pteronyssinus) allergen-like protein from the hard tickIxodes ricinus– a novel member of ML (MD-2-related lipid-recognition) domain protein family
J. HORÁČKOVÁ, N. RUDENKO, M. GOLOVCHENKO, L. GRUBHOFFER
Parasitology.2010; 137(7): 1139. CrossRef
Household Arthropod Allergens in Korea
Tai-Soon Yong, Kyoung Yong Jeong
The Korean Journal of Parasitology.2009; 47(Suppl): S143. CrossRef

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Reactivity of German Cockroach Allergen, Bla g 2, Peptide Fragments to IgE Antibodies in Patients' Sera: Haeseok Lee, Kyoung Yong Jeong, Kwang Hyun Shin, Myung-hee Yi, Darambazar Gantulaga, Chein-Soo Hong, Tai-Soon Yong; Korean J Parasitol 2008;46(4):243-246.
Published online December 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.4.243

Abstract
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Bla g 2 is a cockroach allergen of great importance. This study was conducted to identify IgE-binding epitope(s) of Bla g 2 using the recombinant protein technique. Approximately 50% of tested sera showed IgE reactivity to Pichia-expressed Bla g 2 (PrBla g 2) and E. coli-expressed Bla g 2 (ErBla g 2). Only 5.3% of serum samples showed stronger reactivity to PrBla g 2 than ErBla g 2, indicating that serum was reactive to conformational or carbohydrate epitopes. The full-length and 5 peptide fragments of Bla g 2 were produced in E. coli. All fragments showed IgE-binding activity to the cockroach-allergy patients' sera. Specifically, peptide fragments of amino acid residue 1-75 and 146-225 appeared to be important for IgE-binding. The information about the IgE-binding epitope of Bla g 2 can aid in the diagnosis and treatment for cockroach allergies.

Citations

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Cross-reactive IgE responses to cockroach, house dust mite, and seafood allergens in patients with allergic rhinitis
Sakinah Mohamad, V Sha Kri Eh Dam, Asma Abdullah Nurul, Fook Tim Chew, Baharudin Abdullah
Expert Review of Clinical Immunology.2025; 21(9): 1307. CrossRef
Edible insects as ingredients in food products: nutrition, functional properties, allergenicity of insect proteins, and processing modifications
Jing Yang, Shuling Zhou, Hong Kuang, Chunhong Tang, Jiajia Song
Critical Reviews in Food Science and Nutrition.2024; 64(28): 10361. CrossRef
Cockroach allergen exposure and risk of asthma
D. C. Do, Y. Zhao, P. Gao
Allergy.2016; 71(4): 463. CrossRef
Pulmonary α-1,3-Glucan–Specific IgA-Secreting B Cells Suppress the Development of Cockroach Allergy
Preeyam S Patel, R Glenn King, John F Kearney
The Journal of Immunology.2016; 197(8): 3175. CrossRef
IgE-Binding Epitope Mapping and Tissue Localization of the Major American Cockroach Allergen Per a 2
Mey-Fann Lee, Chia-Wei Chang, Pei-Pong Song, Guang-Yuh Hwang, Shyh-Jye Lin, Yi-Hsing Chen
Allergy, Asthma & Immunology Research.2015; 7(4): 376. CrossRef
Different Bla‐g T cell antigens dominate responses in asthma versus rhinitis subjects
M. B. C. Dillon, V. Schulten, C. Oseroff, S. Paul, L. M. Dullanty, A. Frazier, X. Belles, M.‐D. Piulachs, C. Visness, L. Bacharier, G. R. Bloomberg, P. Busse, J. Sidney, B. Peters, A. Sette
Clinical & Experimental Allergy.2015; 45(12): 1856. CrossRef
Preparation and Characterization of an Extract of German Cockroach From a Korean Source
Kyoung Yong Jeong, Soo-Young Choi, Jae-Hyun Lee, Joo-Shil Lee, Tai-Soon Yong, Chein-Soo Hong, Jung-Won Park
Allergy, Asthma & Immunology Research.2013; 5(2): 102. CrossRef
Identification of Novel Allergenic Components from German Cockroach Fecal Extract by a Proteomic Approach
Kyoung Yong Jeong, Chung-ryul Kim, Jina Park, In-Soo Han, Jung-Won Park, Tai-Soon Yong
International Archives of Allergy and Immunology.2013; 161(4): 315. CrossRef
The Cockroach and Allergic Diseases
Myung Hyun Sohn, Kyu-Earn Kim
Allergy, Asthma & Immunology Research.2012; 4(5): 264. CrossRef
Validation of a Phage Display and Computational Algorithm by Mapping a Conformational Epitope of Bla g 2
Ruby Tiwari, Surendra S. Negi, Benjamin Braun, Werner Braun, Anna Pomés, Martin D. Chapman, Randall M. Goldblum, Terumi Midoro-Horiuti
International Archives of Allergy and Immunology.2012; 157(4): 323. CrossRef
Sensitization to per a 2 of the American cockroach correlates with more clinical severity among airway allergic patients in Taiwan
Mey-Fann Lee, Pei-Peng Song, Guang-Yuh Hwang, Shyh-Jye Lin, Yi-Hsing Chen
Annals of Allergy, Asthma & Immunology.2012; 108(4): 243. CrossRef
Household Arthropod Allergens in Korea
Tai-Soon Yong, Kyoung Yong Jeong
The Korean Journal of Parasitology.2009; 47(Suppl): S143. CrossRef

8,572 View
86 Download
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Persisting antibody reaction in paragonimiasis after praziquantel treatment is elicited mainly by egg antigens: Seung-Yull Cho, Yoon Kong, Doo-Hee Yun, Shin-Yong Kang, Lee-Soo Kim, Young-Bae Chung, Hyun-Jong Yang; Korean J Parasitol 2000;38(2):75-84.
Published online June 30, 2000; DOI: https://doi.org/10.3347/kjp.2000.38.2.75

Abstract
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Antibody responses in serum and cerebrospinal fluid (CSF) samples from patients with active and chronic paragonimiasis and in sera from patients on whom follow-up studies were done after praziquantel treatment were analyzed using antigens of Paragonimus westermani prepared from eggs, metacercariae, juveniles of 4- and 7-week old, adult worms and recombinant protein of 28 kDa cruzipain-like cysteine protease (rPw28CCP). The patient sera/CSFs of active and chronic paragonimiasis revealed strong antibody reactions against the crude extracts of 4- and 7-week old juveniles as well as against those from egg and adult. rPw28CCP also showed specific reaction to the sera with active paragonimiasis. After the treatment, levels of specific antibodies in the sera gradually decreased to negative range in most patients. In some cases with persisting high antibody levels, however, the reactions at 27 kDa egg protein were sustained throughout the observation period of 34 months. The reactions at 35 and 32 kDa in adult extract and rPw28CCP disappeared rapidly after the treatment. Persistent antibody reactions even after successful treatment are provoked by continuous antigenic challenge from eggs which were not resolved by treatment.

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Y.-A. BAE, S.-H. KIM, C.-S. AHN, J.-G. KIM, Y. KONG
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Monoclonal antibodies to recombinant Der p 2, a major house dust mite allergen: specificity, epitope analysis and development of two-site capture ELISA: Tai-Soon Yong, Sang-Mi Lee, Gab-Man Park, In-Yong Lee, Han-Il Ree, Kyung-Sup Kim, Sang-Hwan Oh, Jung-Won Park, Chein-Soo Hong; Korean J Parasitol 1999;37(3):163-169.
Published online September 20, 1999; DOI: https://doi.org/10.3347/kjp.1999.37.3.163

Abstract
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House dust mite allergens have been well established as sensitizing agents that are important in the induction of allergic diseases. In order to analyze epitopes of the allergen and to develop a quantitative method of the allergen exposure, monoclonal antibodies against a recombinant Der p 2 (rDer p 2), one of the major allergens of Dermatophagoides pteronyssinus, were produced. Four monoclonal antibodies produced were species-specific and did not cross-react to the D. farinae crude extract. Two of the monoclonal antibodies were found to be IgG1 and the others were IgM. For the analysis of epitopes, a Der p 2 cDNA encoding 126 amino acids (aa) was dissected into three fragments with several overlapping peptides, A (aa residues 1-49), B (44-93), and C fragment (84-126). Three monoclonal antibodies showed reactivities to the recombinant B fragment and to the full-length rDer p 2, but one monoclonal antibody reacted only with the full-length rDer p 2. Two-site capture ELISA was developed using two different monoclonal antibodies for quantitating Der p 2 in house dust. The sensitivity limit was 4 ng/ml with rDer p 2 and 8 ?g/ml with the D. pteronyssinus crude extract. The result suggested that the assay using monoclonal antibodies against rDer p 2 could be useful for the environmental studies and for the standardization of mite allergen extracts.

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