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Brief Communication

Partial characterization of a cysteine protease inhibitor of Plasmodium vivax
Tuấn Cường Võ, Jung-Mi Kang, Hương Giang Lê, Byoung-Kuk Na
Parasites Hosts Dis 2025;63(4):354-359.
Published online November 19, 2025
DOI: https://doi.org/10.3347/PHD.25043
Cysteine proteases play key roles in the biology of Plasmodium parasites and are recognized as antimalarial drug targets. Because these enzymes are involved in diverse biological functions, precise regulation is required to prevent unnecessary damage to both parasites and hosts. In this study, we identified an endogenous inhibitor of cysteine protease of Plasmodium vivax (PvICP) and characterized its biochemical properties. PvICP was found to share highly similar structural characteristics with orthologous proteins from other Plasmodium species. Recombinant PvICP (rPvICP) expressed in Escherichia coli showed a broad range of inhibitory activity against falcipain family cysteine proteases, including vivapain-3, vivapain-4, falcipain-3, malapain-2, and malapain-4, with more potent inhibitory activity against vivapain-3 and vivapain-4. rPvICP’s inhibitory activity was not significantly affected by pH, suggesting its broad biological functions. These findings provide new insights into PvICP and lay the groundwork for future studies exploring its biological significance and potential as a therapeutic target in malaria research.
  • 271 View
  • 16 Download

Original Articles

Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN)
Thassanee Yuthithum, Orawan Phuphisut, Onrapak Reamtong, Nathamon Kosoltanapiwat, Salisa Chaimon, Porntida Kobpornchai, Charin Thawornkuno, Preeyarat Malaithong, Orathai Sawatdichaikul, Poom Adisakwattana
Parasites Hosts Dis 2024;62(3):330-341.
Published online August 26, 2024
DOI: https://doi.org/10.3347/PHD.24026
The Trichinella spiralis novel cystatin (TsCstN) inhibits cathepsin L (CatL) activity and inflammation of macrophages during lipopolysaccharide (LPS) induction. To identify the protease inhibitory region, this study applied an in silico modeling approach to simulate truncation sites of TsCstN (Ts01), which created four truncated forms, including TsCstN∆1-39 (Ts02), TsCstN∆1-71 (Ts03), TsCstN∆1-20, ∆73-117 (Ts04), and TsCstN∆1-20, ∆42-117 (Ts05). The superimposition of these truncates modeled with AlphaFold Colab indicated that their structures were more akin to Ts01 than those modeled with I-TASSER. Moreover, Ts04 exhibited the closest resemblance to the structure of Ts01. The recombinant Ts01 (rTs01) and truncated proteins (rTs02, rTs03, and rTs04) were successfully expressed in a prokaryotic expression system while Ts05 was synthesized, with sizes of approximately 14, 12, 8, 10, and 2.5 kDa, respectively. When determining the inhibition of CatL activity, both rTs01 and rTs04 effectively reduced CatL activity in vitro. Thus, the combination of the α1 and L1 regions may be sufficient to inhibit CatL. This study provides comprehensive insights into TsCstN, particularly regarding its protein function and inhibitory domains against CatL.

Citations

Citations to this article as recorded by  Crossref logo
  • Systems biology of Haemonchus contortus – Advancing biotechnology for parasitic nematode control
    Yuanting Zheng, Neil D. Young, Tao Wang, Bill C.H. Chang, Jiangning Song, Robin B. Gasser
    Biotechnology Advances.2025; 81: 108567.     CrossRef
  • Therapeutic potentials of Trichinella spiralis in immune disorders: From allergy to autoimmunity
    Minkyoung Cho, Hak Sun Yu
    Parasites, Hosts and Diseases.2025; 63(2): 123.     CrossRef
  • 2,594 View
  • 71 Download
  • 2 Web of Science
  • Crossref
Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii
Yeonchul Hong, Jung-Mi Kang, So-Young Joo, Su-Min Song, H??ng Giang L?, Th? Lam Th?i, Jinyoung Lee, Youn-Kyoung Goo, Dong-Il Chung, Woon-Mok Sohn, Byoung-Kuk Na
Korean J Parasitol 2018;56(5):409-418.
Published online October 31, 2018
DOI: https://doi.org/10.3347/kjp.2018.56.5.409
Acanthamoeba spp. are free-living protozoa that are opportunistic pathogens for humans. Cysteine proteases of Acanthamoeba have been partially characterized, but their biochemical and functional properties are not clearly understood yet. In this study, we isolated a gene encoding cysteine protease of A. castellanii (AcCP) and its biochemical and functional properties were analyzed. Sequence analysis of AcCP suggests that this enzyme is a typical cathepsin L family cysteine protease, which shares similar structural characteristics with other cathepsin L-like enzymes. The recombinant AcCP showed enzymatic activity in acidic conditions with an optimum at pH 4.0. The recombinant enzyme effectively hydrolyzed human proteins including hemoglobin, albumin, immunoglobuins A and G, and fibronectin at acidic pH. AcCP mainly localized in lysosomal compartment and its expression was observed in both trophozoites and cysts. AcCP was also identified in cultured medium of A. castellanii. Considering to lysosomal localization, secretion or release by trophozoites and continuous expression in trophozoites and cysts, the enzyme could be a multifunctional enzyme that plays important biological functions for nutrition, development and pathogenicity of A. castellanii. These results also imply that AcCP can be a promising target for development of chemotherapeutic drug for Acanthamoeba infections.

Citations

Citations to this article as recorded by  Crossref logo
  • Acanthamoeba castellanii cysteine protease 3 promotes M1 macrophage polarization through the TLR4/NF‑κB pathway
    Zhi-xin Wang, Wan-jun Jiao, Mian-jing Wang, Yong Yang, Hai-long Wang, Hong-li Liu
    Parasites & Vectors.2025;[Epub]     CrossRef
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    Eva Zanditenas, Serge Ankri
    Virulence.2024;[Epub]     CrossRef
  • Epidemiology of and Genetic Factors Associated with Acanthamoeba Keratitis
    Muhammad Ilyas, Fiona Stapleton, Mark D. P. Willcox, Fiona Henriquez, Hari Kumar Peguda, Binod Rayamajhee, Tasbiha Zahid, Constantinos Petsoglou, Nicole A. Carnt
    Pathogens.2024; 13(2): 142.     CrossRef
  • Staurosporine as a Potential Treatment for Acanthamoeba Keratitis Using Mouse Cornea as an Ex Vivo Model
    Rubén L. Rodríguez-Expósito, Ines Sifaoui, Lizbeth Salazar-Villatoro, Carlos J. Bethencourt-Estrella, José J. Fernández, Ana R. Díaz-Marrero, Robert Sutak, Maritza Omaña-Molina, José E. Piñero, Jacob Lorenzo-Morales
    Marine Drugs.2024; 22(9): 423.     CrossRef
  • The gene expression and proteomic profiling of Acanthamoeba isolates
    Chayan Sharma, Sumeeta Khurana, Alka Bhatia, Amit Arora, Amit Gupta
    Experimental Parasitology.2023; 255: 108630.     CrossRef
  • Biological characteristics and pathogenicity of Acanthamoeba
    Yuehua Wang, Linzhe Jiang, Yitong Zhao, Xiaohong Ju, Le Wang, Liang Jin, Ryan D. Fine, Mingguang Li
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Induction of Programmed Cell Death in Acanthamoeba culbertsoni by the Repurposed Compound Nitroxoline
    Rubén L. Rodríguez-Expósito, Ines Sifaoui, María Reyes-Batlle, Frieder Fuchs, Patrick L. Scheid, José E. Piñero, Robert Sutak, Jacob Lorenzo-Morales
    Antioxidants.2023; 12(12): 2081.     CrossRef
  • Paradigms of Protist/Bacteria Symbioses Affecting Human Health: Acanthamoeba species and Trichomonas vaginalis
    Fiona L. Henriquez, Ronnie Mooney, Timothy Bandel, Elisa Giammarini, Mohammed Zeroual, Pier Luigi Fiori, Valentina Margarita, Paola Rappelli, Daniele Dessì
    Frontiers in Microbiology.2021;[Epub]     CrossRef
  • Trogocytosis in Unicellular Eukaryotes
    Kumiko Nakada-Tsukui, Tomoyoshi Nozaki
    Cells.2021; 10(11): 2975.     CrossRef
  • Insight into the Lifestyle of Amoeba Willaertia magna during Bioreactor Growth Using Transcriptomics and Proteomics
    Issam Hasni, Philippe Decloquement, Sandrine Demanèche, Rayane Mouh Mameri, Olivier Abbe, Philippe Colson, Bernard La Scola
    Microorganisms.2020; 8(5): 771.     CrossRef
  • Identification and biochemical characterisation of Acanthamoeba castellanii cysteine protease 3
    Zhixin Wang, Duo Wu, Hiroshi Tachibana, Meng Feng, Xun-jia Cheng
    Parasites & Vectors.2020;[Epub]     CrossRef
  • Host Invasion by Pathogenic Amoebae: Epithelial Disruption by Parasite Proteins
    Abigail Betanzos, Cecilia Bañuelos, Esther Orozco
    Genes.2019; 10(8): 618.     CrossRef
  • 8,362 View
  • 168 Download
  • 13 Web of Science
  • Crossref

Mini Review

Serine Proteases of Parasitic Helminths
Yong Yang, Yun jun Wen, Ya Nan Cai, Isabelle Vall?e, Pascal Boireau, Ming Yuan Liu, Shi Peng Cheng
Korean J Parasitol 2015;53(1):1-11.
Published online February 27, 2015
DOI: https://doi.org/10.3347/kjp.2015.53.1.1

Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development and nutrition, host tissues and cell invasion, anticoagulation, and immune evasion. In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni). Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

Citations

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  • N-terminomics profiling of host proteins targeted by excretory-secretory proteases of the nematode Angiostrongylus vasorum identifies points of interaction with canine coagulation and complement cascade
    Nina Germitsch, Tobias Kockmann, Manuela Schnyder, Lucienne Tritten, Elham Kazemirad
    PLOS ONE.2025; 20(1): e0316217.     CrossRef
  • Administration of Trichinella spiralis Antigens Alleviated Diabetic Nephropathy in Diabetic Mice
    Asmaa M. El-kady, Sarah A. Altwaim, Haleema H. Albohiri, Majed H. Wakid, Khalil Mohamed, Eman Abdullah Alshehri, Hayam Elshazly, Hatem A. Elshabrawy, Dina hamed
    Acta Parasitologica.2025;[Epub]     CrossRef
  • Characterization of a novel invasive virulence of chymotrypsin-like elastase family member 2A from Trichinella spiralis
    Xin Guo, Xin Zhuo Zhang, Yao Zhang, Ru Zhang, Shao Rong Long, Ruo Dan Liu, Jing Cui, Zhong Quan Wang
    Acta Tropica.2025; 270: 107803.     CrossRef
  • Paying attention to attention: High attention sites as indicators of protein family and function in language models
    Gowri Nayar, Alp Tartici, Russ B. Altman, Serdar Bozdag
    PLOS Computational Biology.2025; 21(9): e1013424.     CrossRef
  • Regulatory and coding changes underlying development and host detection in vertebrate-parasitizing blowflies
    Pedro Mariano-Martins, Diniz Lima Ferreira, Vanessa Araujo Soares da Cunha, Carolina Kurotusch Canettieri, Letícia Chiara Baldassio de Paula, Tatiana Teixeira Torres
    International Journal for Parasitology.2025;[Epub]     CrossRef
  • Trichinella spiralis serine protease mediates larval invasion of gut epithelium via binding to CK8 and activating RhoA/ROCK1 pathway
    Wen Wen Zheng, Xin Zhuo Zhang, Pei Kun Cong, Ru Zhang, Shao Rong Long, Xi Zhang, Ruo Dan Liu, Zhong Quan Wang, Jing Cui, Feng Xue
    PLOS Neglected Tropical Diseases.2025; 19(11): e0013725.     CrossRef
  • Host-parasite interactions: a study on the pathogenicity of different Mesanophrys sp. densities and hemocytes-mediated parasitic resistance of swimming crabs (Portunus trituberculatus)
    Lujia Yang, Ruiling Zhou, Chunlin Wang, Xiao Xie, Suming Zhou, Fei Yin
    Parasitology Research.2024;[Epub]     CrossRef
  • Serine protease mediates Ovomermis sinensis‐inhibited host immune responses by inducing apoptosis: implications for successful parasitism and host mortality
    Zhenlong Jiao, Mingming Chen, Wenjing Zhao, Yuanming Wu, Guo Guo
    Pest Management Science.2024; 80(4): 1968.     CrossRef
  • Application of a recombinant novel trypsin from Trichinella spiralis for serodiagnosis of trichinellosis
    Lu Lu Han, Qi Qi Lu, Yang Li Li, Wen Wen Zheng, Pian Ren, Ruo Dan Liu, Jing Cui, Zhong Quan Wang
    Parasites & Vectors.2024;[Epub]     CrossRef
  • A novel Trichinella spiralis serine proteinase disrupted gut epithelial barrier and mediated larval invasion through binding to RACK1 and activating MAPK/ERK1/2 pathway
    Yan Yan Song, Xin Zhuo Zhang, Bo Ning Wang, Yong Kang Cheng, Xin Guo, Xi Zhang, Shao Rong Long, Ruo Dan Liu, Zhong Quan Wang, Jing Cui, Krystyna Cwiklinski
    PLOS Neglected Tropical Diseases.2024; 18(1): e0011872.     CrossRef
  • Salmon louse labial gland enzymes: implications for host settlement and immune modulation
    Helena Marie Doherty Midtbø, Christiane Eichner, Lars Are Hamre, Michael Dondrup, Linn Flesland, Kristoffer Helland Tysseland, Heidi Kongshaug, Andreas Borchel, Renate Hvidsten Skoge, Frank Nilsen, Aina-Cathrine Øvergård
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  • Moonlighting on the Fasciola hepatica tegument: Enolase, a glycolytic enzyme, interacts with the extracellular matrix and fibrinolytic system of the host
    Eve O’Kelly, Krystyna Cwiklinski, Carolina De Marco Verissimo, Nichola Eliza Davies Calvani, Jesús López Corrales, Heather Jewhurst, Andrew Flaus, Richard Lalor, Judit Serrat, John P. Dalton, Javier González-Miguel, Gabriel Rinaldi
    PLOS Neglected Tropical Diseases.2024; 18(8): e0012069.     CrossRef
  • Excreted/Secreted 15-kDa Proteins and Serine Protease Peptides from Haemonchus contortus Act as Immune-Response Enhancers in Lambs
    René Camas-Pereyra, Génesis Andrea Bautista-García, Gustavo Pérez-Anzúrez, Zaira Carolina Duran-Cortes, David Emanuel Reyes-Guerrero, Jocelyn Maza-Lopez, Agustín Olmedo-Juárez, María Eugenia López-Arellano
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    Orken S. Akibekov, Aissarat M. Gajimuradova, Alfiya S. Syzdykova, Aibek Kh. Zhumalin, Fariza S. Zhagipar, Fabio Tosini, Zhannara Zh. Akanova, Nurtai N. Gubaidullin, Nasipkhan A. Askarova
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  • Trypsin, chymotrypsin and elastase in health and disease
    Oladoyin Grace Famutimi, Victor Gbolahan Adebiyi, Bukola Grace Akinmolu, Omoniyi Vincent Dada, Isaac Olusanjo Adewale
    Future Journal of Pharmaceutical Sciences.2024;[Epub]     CrossRef
  • Protein profile of extracellular vesicles derived from adult Parascaris spp.
    Vishnu Manikantan, Nichol E. Ripley, Martin K. Nielsen, Sriveny Dangoudoubiyam
    Parasites & Vectors.2024;[Epub]     CrossRef
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    René Camas-Pereyra, Génesis A. Bautista-García, Guillermina Avila, Yazmin Alcala-Canto, Jocelyn Maza-Lopez, David E. Reyes-Guerrero, Rosa Isabel Higuera-Piedrahita, María Eugenia López-Arellano
    Molecular and Biochemical Parasitology.2023; 253: 111545.     CrossRef
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    Kristyna Peterkova, Jiri Vorel, Jana Ilgova, Pavel Ostasov, Pavla Fajtova, Lukas Konecny, Marta Chanova, Martin Kasny, Martin Horn, Jan Dvorak
    International Journal for Parasitology.2023; 53(5-6): 253.     CrossRef
  • Secreted peptidases contribute to virulence of fish pathogen Flavobacterium columnare
    Nicole C. Thunes, Haitham H. Mohammed, Jason P. Evenhuis, Ryan S. Lipscomb, David Pérez-Pascual, Rebecca J. Stevick, Clayton Birkett, Rachel A. Conrad, Jean-Marc Ghigo, Mark J. McBride
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  • Biological control 2.0: Use of nematophagous fungi enzymes for nematode control
    Filippe Elias de Freitas Soares, Juliana Marques Ferreira, Hugo Leonardo André Genier, Laith Khalil Tawfeeq Al-Ani, Liliana Aguilar-Marcelino
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  • In vitro knockdown of TsDNase II-7 suppresses Trichinella spiralis invasion into the host’s intestinal epithelial cells
    Jing Wang, Xuemin Jin, Chengyao Li, Xinhui Chen, Yanfeng Li, Mingyuan Liu, Xiaolei Liu, Jing Ding, Pamela Marie Pennington
    PLOS Neglected Tropical Diseases.2023; 17(6): e0011323.     CrossRef
  • An insight into the functional genomics and species classification of Eudiplozoon nipponicum (Monogenea, Diplozoidae), a haematophagous parasite of the common carp Cyprinus carpio
    Jiří Vorel, Nikol Kmentová, Christoph Hahn, Petr Bureš, Martin Kašný
    BMC Genomics.2023;[Epub]     CrossRef
  • The gut microbiota contributes to changes in the host immune response induced by Trichinella spiralis
    Chengyao Li, Yi Liu, Xiaolei Liu, Xue Bai, Xuemin Jin, Fengyan Xu, Hong Chen, Yuanyuan Zhang, Isabelle Vallee, Mingyuan Liu, Yong Yang, Krystyna Cwiklinski
    PLOS Neglected Tropical Diseases.2023; 17(8): e0011479.     CrossRef
  • Molecular characterization of a novel serine proteinase from Trichinella spiralis and its participation in larval invasion of gut epithelium
    Yan Yan Song, Xin Zhuo Zhang, Bo Ning Wang, Min Min Weng, Zhao Yu Zhang, Xin Guo, Xi Zhang, Zhong Quan Wang, Jing Cui, jong-Yil Chai
    PLOS Neglected Tropical Diseases.2023; 17(9): e0011629.     CrossRef
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    Xin Zhuo Zhang, Wen Wen Yue, Sheng Jie Bai, Hui Nan Hao, Yan Yan Song, Shao Rong Long, Ruo Dan Liu, Jing Cui, Zhong Quan Wang
    Acta Tropica.2022; 226: 106263.     CrossRef
  • Comparative transcriptome profiles of Schistosoma japonicum larval stages: Implications for parasite biology and host invasion
    Shaoyun Cheng, Bingkuan Zhu, Fang Luo, Xiying Lin, Chengsong Sun, Yanmin You, Cun Yi, Bin Xu, Jipeng Wang, Yan Lu, Wei Hu, James Cotton
    PLOS Neglected Tropical Diseases.2022; 16(1): e0009889.     CrossRef
  • Characterization of the genome and serine protease of a novel Bacillus subtilis isolate
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    Paritosh Joshi, Prasanta Kumar K. Mishra
    Acta Parasitologica.2022; 67(2): 619.     CrossRef
  • Proteomic Profiling and In Silico Characterization of the Secretome of Anisakis simplex Sensu Stricto L3 Larvae
    Maciej Kochanowski, Joanna Dąbrowska, Mirosław Różycki, Jacek Sroka, Jacek Karamon, Aneta Bełcik, Weronika Korpysa-Dzirba, Tomasz Cencek
    Pathogens.2022; 11(2): 246.     CrossRef
  • Transcriptomic Analysis of Steinernema Nematodes Highlights Metabolic Costs Associated to Xenorhabdus Endosymbiont Association and Rearing Conditions
    Emilie Lefoulon, John G. McMullen, S. Patricia Stock
    Frontiers in Physiology.2022;[Epub]     CrossRef
  • Proteases secreted by Trichinella spiralis intestinal infective larvae damage the junctions of the intestinal epithelial cell monolayer and mediate larval invasion
    Yan Yan Song, Qi Qi Lu, Lu Lu Han, Shu Wei Yan, Xin Zhuo Zhang, Ruo Dan Liu, Shao Rong Long, Jing Cui, Zhong Quan Wang
    Veterinary Research.2022;[Epub]     CrossRef
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    International Journal of Molecular Sciences.2022; 23(8): 4336.     CrossRef
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    Developmental & Comparative Immunology.2021; 114: 103820.     CrossRef
  • A critical review on marine serine protease and its inhibitors: A new wave of drugs?
    Noora Barzkar, Zahoor Khan, Saeid Tamadoni Jahromi, Sajjad Pourmozaffar, Mohsen Gozari, Reza Nahavandi
    International Journal of Biological Macromolecules.2021; 170: 674.     CrossRef
  • Proteomic analysis of hydrolytic proteases in excretory/secretory proteins from Trichinella spiralis intestinal infective larvae using zymography combined with shotgun LC-MS/MS approach
    Hua Nan Ren, Tong Xu Zhuo, Sheng Jie Bai, Ying Bai, Xiang Yuan Sun, Ruo Dan Liu, Shao Rong Long, Jing Cui, Zhong Quan Wang
    Acta Tropica.2021; 216: 105825.     CrossRef
  • Disruption of Epithelial Barrier of Caco-2 Cell Monolayers by Excretory Secretory Products of Trichinella spiralis Might Be Related to Serine Protease
    Chengyao Li, Xue Bai, Xiaolei Liu, Yuanyuan Zhang, Lei Liu, Lixiao Zhang, Fengyan Xu, Yong Yang, Mingyuan Liu
    Frontiers in Microbiology.2021;[Epub]     CrossRef
  • Immune Protection of a Helminth Protein in the DSS-Induced Colitis Model in Mice
    Shao Rong Long, Ruo Dan Liu, Deepak Vijaya Kumar, Zhong Quan Wang, Chien-Wen Su
    Frontiers in Immunology.2021;[Epub]     CrossRef
  • The immune protection induced by a serine protease from the Trichinella spiralis adult against Trichinella spiralis infection in pigs
    Daoxiu Xu, Xue Bai, Jing Xu, Xuelin Wang, Zijian Dong, Wenjie Shi, Fengyan Xu, Yanfeng Li, Mingyuan Liu, Xiaolei Liu, Hernando A. del Portillo
    PLOS Neglected Tropical Diseases.2021; 15(5): e0009408.     CrossRef
  • Spatial expression pattern of serine proteases in the blood fluke Schistosoma mansoni determined by fluorescence RNA in situ hybridization
    Lenka Ulrychová, Pavel Ostašov, Marta Chanová, Michael Mareš, Martin Horn, Jan Dvořák
    Parasites & Vectors.2021;[Epub]     CrossRef
  • Characterization of a chymotrypsin-like enzyme from Trichinella spiralis and its facilitation of larva penetration into the host's enteral epithelial cells
    Jia Xu, Ruo Dan Liu, Shao Rong Long, Yan Yan Song, Peng Jiang, Xi Zhang, Jing Cui, Zhong Quan Wang
    Research in Veterinary Science.2020; 128: 1.     CrossRef
  • In silico design of a T-cell epitope vaccine candidate for parasitic helminth infection
    Ayat Zawawi, Ruth Forman, Hannah Smith, Iris Mair, Murtala Jibril, Munirah H. Albaqshi, Andrew Brass, Jeremy P. Derrick, Kathryn J. Else, Maria Elena Bottazzi
    PLOS Pathogens.2020; 16(3): e1008243.     CrossRef
  • Effect of recombinant serine protease from adult stage of Trichinella spiralis on TNBS-induced experimental colitis in mice
    Jianda Pang, Jing Ding, Lixiao Zhang, Yuanyuan Zhang, Yaming Yang, Xue Bai, Xiaolei Liu, Xuemin Jin, Heng Guo, Yong Yang, Mingyuan Liu
    International Immunopharmacology.2020; 86: 106699.     CrossRef
  • Binding of elastase-1 and enterocytes facilitates Trichinella spiralis larval intrusion of the host's intestinal epithelium
    Chen Xi Hu, Jie Zeng, Da Qi Yang, Xin Yue, Ruo Dan Liu, Shao Rong Long, Xi Zhang, Peng Jiang, Jing Cui, Zhong Quan Wang
    Acta Tropica.2020; 211: 105592.     CrossRef
  • Effect of recombinant serine protease from newborn larval stage of Trichinella spiralis on 2,4,6-trinitrobenzene sulfonic acid-induced experimental colitis in mice
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Original Article

Diagnostic Efficacy of a Recombinant Cysteine Protease of Spirometra erinacei Larvae for Serodiagnosis of Sparganosis
S.M. Mazidur Rahman, Jae-Hwan Kim, Sung-Tae Hong, Min-Ho Choi
Korean J Parasitol 2014;52(1):41-46.
Published online February 19, 2014
DOI: https://doi.org/10.3347/kjp.2014.52.1.41

The mature domain of a cysteine protease of Spirometra erinacei plerocercoid larva (i.e., sparganum) was expressed in Escherichia coli, and its value as an antigen for the serodiagnosis of sparganosis was investigated. The recombinant protein (rSepCp-1) has the molecular weight of 23.4 kDa, and strongly reacted with the sparganum positive human or mice sera but not with negative sera by immunoblotting. ELISA with rSepCp-1 protein or sparganum crude antigen (SeC) was evaluated for the serodiagnosis of sparganosis using patient's sera. The sensitivity and specificity of ELISA using rSepCp-1 protein were 95.0% (19/20) and 99.1% (111/112), respectively. In contrast, the sensitivity and specificity of ELISA with SeC were 100% (20/20) and 96.4% (108/112), respectively. Moreover, in experimentally infected mice, the sensitivity and specificity of both ELISA assays were 100% for the detection of anti-sparganum IgG. It is suggested that the rSepCp-1 protein-based ELISA could provide a highly sensitive and specific assay for the diagnosis of sparganosis.

Citations

Citations to this article as recorded by  Crossref logo
  • Development of an immunochromatographic test for serodiagnosis of human sparganosis
    Jitaporn Harasan, Lakkhana Sadaow, Patcharaporn Boonroumkaew, Rutchanee Rodpai, Oranuch Sanpool, Hiroshi Yamasaki, Pewpan M. Intapan, Wanchai Maleewong
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    Anqi Luo, Shuyu Chen, Mingye He, Xiaoruo Tan, Zhikang Li, Wei Liu, Yisong Liu
    Vector-Borne and Zoonotic Diseases.2024;[Epub]     CrossRef
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    Yusi Chen, Xu Chen, Huicong Kang
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Brief Communications

Partial Purification and Properties of a Cysteine Protease from Citrus Red Mite Panonychus citri
Seong Chul Hong, Kyu-Hee Her, Heung-Up Kim, Jaechun Lee, Sang Pyo Lee, Young-Bae Chung
Korean J Parasitol 2014;52(1):117-120.
Published online February 19, 2014
DOI: https://doi.org/10.3347/kjp.2014.52.1.117

Several studies have reported that the citrus red mites Panonychus citri were an important allergen of citrus-cultivating farmers in Jeju Island. The aim of the present study was to purify and assess properties of a cysteine protease from the mites acting as a potentially pathogenic factor to citrus-cultivating farmers. A cysteine protease was purified using column chromatography of Mono Q anion exchanger and Superdex 200 HR gel filtration. It was estimated to be 46 kDa by gel filtration column chromatography and consisted of 2 polypeptides, at least. Cysteine protease inhibitors, such as trans poxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) and iodoacetic acid (IAA) totally inhibited the enzyme activities, whereas serine or metalloprotease inhibitors did not affect the activities. In addition, the purified enzyme degraded human IgG, collagen, and fibronectin, but not egg albumin. From these results, the cysteine protease of the mites might be involved in the pathogenesis such as tissue destruction and penetration instead of nutrient digestion.

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Expression of Exogenous Human Hepatic Nuclear Factor-1α by a Lentiviral Vector and Its Interactions with Plasmodium falciparum Subtilisin-Like Protease 2
Shunyao Liao, Yunqiang Liu, Bing Zheng, Pyo Yun Cho, Hyun Ok Song, Yun-Seok Lee, Suk-Yul Jung, Hyun Park
Korean J Parasitol 2011;49(4):431-436.
Published online December 16, 2011
DOI: https://doi.org/10.3347/kjp.2011.49.4.431

The onset, severity, and ultimate outcome of malaria infection are influenced by parasite-expressed virulence factors as well as by individual host responses to these determinants. In both humans and mice, liver injury follows parasite entry, persisting to the erythrocytic stage in the case of infection with the fatal strain of Plasmodium falciparum. Hepatic nuclear factor (HNF)-1α is a master regulator of not only the liver damage and adaptive responses but also diverse metabolic functions. In this study, we analyzed the expression of host HNF-1α in relation to malaria infection and evaluated its interaction with the 5'-untranslated region of subtilisin-like protease 2 (subtilase, Sub2). Recombinant human HNF-1α expressed by a lentiviral vector (LV HNF-1α) was introduced into mice. Interestingly, differences in the activity of the 5'-untranslated region of the Pf-Sub2 promoter were detected in 293T cells, and LV HNF-1α was observed to influence promoter activity, suggesting that host HNF-1α interacts with the Sub2 gene.

  • 8,587 View
  • 67 Download

Original Articles

Protease-Activated Receptor 2 Is Involved in Th2 Responses against Trichinella spiralis Infection
Mi Kyung Park, Min Kyoung Cho, Shin Ae Kang, Hye-Kyung Park, Yun Seong Kim, Ki Uk Kim, Soon Cheol Ahn, Dong-Hee Kim, Hak Sun Yu
Korean J Parasitol 2011;49(3):235-243.
Published online September 30, 2011
DOI: https://doi.org/10.3347/kjp.2011.49.3.235

In order to get a better understanding of the role of protease-activated receptor 2 (PAR2) in type 2 helper T (Th2) cell responses against Trichinella spiralis infection, we analyzed Th2 responses in T. spiralis-infected PAR2 knockout (KO) mice. The levels of the Th2 cell-secreted cytokines, IL-4, IL-5, and IL-13 were markedly reduced in the PAR2 KO mice as compared to the wild type mice following infection with T. spiralis. The serum levels of parasite-specific IgE increased significantly in the wild type mice as the result of T. spiralis infection, but this level was not significantly increased in PAR2 KO mice. The expression level of thymic stromal lymphopoietin, IL-25, and eotaxin gene (the genes were recently known as Th2 response initiators) of mouse intestinal epithelial cells were increased as the result of treatment with T. spiralis excretory-secretory proteins. However, the expression of these chemokine genes was inhibited by protease inhibitor treatments. In conclusion, PAR2 might involve in Th2 responses against T. spiralis infection.

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    Shin Ae Kang, Mi-Kyung Park, Min Kyoung Cho, Sang Kyun Park, Min Seong Jang, Bo-Gie Yang, Myoung Ho Jang, Dong-Hee Kim, Hak Sun Yu, Edward Mitre
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Transcriptional Activity of Plasmodium Subtilisin-like Protease 2 (Pf-Sub2) 5'Untranslated Regions and Its Interaction with Hepatocyte Growth Factor
Shunyao Liao, Yunqiang Liu, Suk-Yul Jung, Pyo Yun Cho, Bing Zheng, Hyun Park
Korean J Parasitol 2010;48(4):291-295.
Published online December 16, 2010
DOI: https://doi.org/10.3347/kjp.2010.48.4.291

The onset, severity, and ultimate outcome of malaria infection are influenced by parasite-expressed virulence factors and individual host responses to these determinants. In both humans and mice, liver injury is involved after parasite entry, which persists until the erythrocyte stage after infection with the fatal strain Plasmodium falciparum (Pf). Hepatocyte growth factor (HGF) has strong anti-apoptotic effects in various kinds of cells, and also has diverse metabolic functions. In this work, Pf-subtilisin-like protease 2 (Pf-Sub2) 5'untranslated region (UTR) was analyzed and its transcriptional activity was estimated by luciferase expression. Fourteen TATA boxes were observed but only one Oct-1 and c-Myb were done. In addition, host HGF interaction with Pf-Sub2 was evaluated by co-transfection of HGF- and Pf-Sub2-cloned vector. Interestingly, -1,422/+12 UTR exhibited the strongest luciferase activity but -329 to +12 UTR did not exhibit luciferase activity. Moreover, as compared with the control of unexpressed HGF, the HGF protein suppressed luciferase expression driven by the 5'untranslated region of the Pf-Sub2 promoter. Taken together, it is suggested that HGF controls and interacts with the promoter region of the Pf-Sub2 gene.

Citations

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  • Characterization of the transcriptome and temperature-induced differential gene expression in QPX, the thraustochytrid parasite of hard clams
    Ewelina Rubin, Arnaud Tanguy, Mickael Perrigault, Emmanuelle Pales Espinosa, Bassem Allam
    BMC Genomics.2014;[Epub]     CrossRef
  • 8,943 View
  • 78 Download
  • Crossref
Enzymatic Activities of Allergen Extracts from Three Species of Dust Mites and Cockroaches Commonly Found in Korean Home
Kyoung Yong Jeong, Chungryul Kim, Tai-Soon Yong
Korean J Parasitol 2010;48(2):151-155.
Published online June 17, 2010
DOI: https://doi.org/10.3347/kjp.2010.48.2.151

Allergen extracts from dust mites and cockroaches commonly found in Korean homes were used to evaluate their enzymatic activity as they are believed to influence allergenicity. Allergen extracts were prepared from 3 dust mite species (Dermatophagoides farinae, D. pteronyssinus, and Tyrophagus putrescentiae) and 3 cockroach species (Blattella germanica, Periplaneta americana, and P. fuliginosa) maintained in the Korea National Arthropods of Medical Importance Resource Bank. Proteins were extracted in PBS after homogenization using liquid nitrogen. The activities of various enzymes were investigated using the API Zym system. No significant difference in phosphatase, lipase, or glycosidase activity was observed among the 6 allergen extracts, but much difference was observed in protease activity. Protease activity was assessed in more detail by gelatin zymography and the EnzChek assay. Extract from T. putrescentiae showed the highest protease activity, followed by those of the cockroach extracts. Extracts from D. farinae and D. pteronyssinus showed only weak protease activity. Gelatinolytic activity was detected mainly in a 30-kDa protein in D. farinae, a 28-kDa protein in D. pteronyssinus, a > 26-kDa protein in T. putrescentiae, a > 20-kDa protein in B. germanica, and a > 23-kDa protein in P. americana and P. fuliginosa. The information on various enzymatic activities obtained in this study may be useful for future studies. In particular, the strong protease activity found in cockroach extracts could contribute to sensitization to cockroach allergens, which is known to be associated with the development of asthma.

Citations

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  • B-cell antibody class switchings are pressuromodulated events: Part II, gene recombination
    Hemant Sarin
    Translational Medicine Communications.2018;[Epub]     CrossRef
  • Allergenic Characterization of a Novel Allergen, Homologous to Chymotrypsin, from German Cockroach
    Kyoung Yong Jeong, Mina Son, Jae-Hyun Lee, Chein-Soo Hong, Jung-Won Park
    Allergy, Asthma & Immunology Research.2015; 7(3): 283.     CrossRef
  • Current Status of Standardization of Inhalant Allergen Extracts in Korea
    Kyoung Yong Jeong, Jae-Hyun Lee, Eun-Jin Kim, Joo-Shil Lee, Sang-Heon Cho, Soo-Jong Hong, Jung-Won Park
    Allergy, Asthma & Immunology Research.2014; 6(3): 196.     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
  • The Effects of Storage Conditions on the Stability of House Dust Mite Extracts
    Kyoung Yong Jeong, Soo-Young Choi, In-Soo Han, Jae-Hyun Lee, Joo-Shil Lee, Chein-Soo Hong, Jung-Won Park
    Allergy, Asthma & Immunology Research.2013; 5(6): 397.     CrossRef
  • House Dust Mite Allergy in Korea: The Most Important Inhalant Allergen in Current and Future
    Kyoung Yong Jeong, Jung-Won Park, Chein-Soo Hong
    Allergy, Asthma & Immunology Research.2012; 4(6): 313.     CrossRef
  • Role of Cockroach Proteases in Allergic Disease
    Kristen Page
    Current Allergy and Asthma Reports.2012; 12(5): 448.     CrossRef
  • Optimization of Allergen Standardization
    Kyoung Yong Jeong, Chein-Soo Hong, Joo-Shil Lee, Jung-Won Park
    Yonsei Medical Journal.2011; 52(3): 393.     CrossRef
  • 9,144 View
  • 82 Download
  • Crossref

Mini Review

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

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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  • Clonorchis sinensis ESPs enhance the activation of hepatic stellate cells by a cross-talk of TLR4 and TGF-β/Smads signaling pathway
    Bo Li, Chao Yan, Jing Wu, Koda Stephane, Xin Dong, Yu-Zhao Zhang, Yu Zhang, Qian Yu, Kui-Yang Zheng
    Acta Tropica.2020; 205: 105307.     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
  • Clonorchiasis
    Men-Bao Qian, Jürg Utzinger, Jennifer Keiser, Xiao-Nong Zhou
    The Lancet.2016; 387(10020): 800.     CrossRef
  • Current status and perspectives of Clonorchis sinensis and clonorchiasis: epidemiology, pathogenesis, omics, prevention and control
    Ze-Li Tang, Yan Huang, Xin-Bing Yu
    Infectious Diseases of Poverty.2016;[Epub]     CrossRef
  • Clonorchis sinensis, an oriental liver fluke, as a human biological agent of cholangiocarcinoma: a brief review
    Tong-Soo Kim, Jhang Ho Pak, Jong-Bo Kim, Young Yil Bahk
    BMB Reports.2016; 49(11): 590.     CrossRef
  • Clonorchis sinensis acetoacetyl-CoA thiolase: identification and characterization of its potential role in surviving in the bile duct
    Jinsi Lin, Hongling Qu, Guishan Chen, Lei He, Yanquan Xu, Zhizhi Xie, Mengyu Ren, Jiufeng Sun, Shan Li, Wenjun Chen, Xueqing Chen, Xiaoyun Wang, Xuerong Li, Chi Liang, Yan Huang, Xinbing Yu
    Parasites & Vectors.2015;[Epub]     CrossRef
  • Clonorchis sinensis ferritin heavy chain triggers free radicals and mediates inflammation signaling in human hepatic stellate cells
    Qiang Mao, Zhizhi Xie, Xiaoyun Wang, Wenjun Chen, Mengyu Ren, Mei Shang, Huali Lei, Yanli Tian, Shan Li, Pei Liang, Tingjin Chen, Chi Liang, Jin Xu, Xuerong Li, Yan Huang, Xinbing Yu
    Parasitology Research.2015; 114(2): 659.     CrossRef
  • Biochemical and immunological characterization of annexin B30 from Clonorchis sinensis excretory/secretory products
    Lei He, Mengyu Ren, Xueqing Chen, Xiaoyun Wang, Shan Li, Jinsi Lin, Chi Liang, Pei Liang, Yue Hu, Huali Lei, Meng Bian, Yan Huang, Zhongdao Wu, Xuerong Li, Xinbing Yu
    Parasitology Research.2014; 113(7): 2743.     CrossRef
  • Identification, immunolocalization, and characterization analyses of an exopeptidase of papain superfamily, (cathepsin C) from Clonorchis sinensis
    Pei Liang, Lei He, Yanquan Xu, Xueqing Chen, Yan Huang, Mengyu Ren, Chi Liang, Xuerong Li, Jin Xu, Gang Lu, Xinbing Yu
    Parasitology Research.2014; 113(10): 3621.     CrossRef
  • Proteomic identification of potential Clonorchis sinensis excretory/secretory products capable of binding and activating human hepatic stellate cells
    Xiaoyun Wang, Fengyu Hu, Xuchu Hu, Wenjun Chen, Yan Huang, Xinbing Yu
    Parasitology Research.2014; 113(8): 3063.     CrossRef
  • Characterization of the secreted cathepsin B cysteine proteases family of the carcinogenic liver fluke Clonorchis sinensis
    Wenjun Chen, Xiaoyun Wang, Xiaoli Lv, Yanli Tian, Yanquan Xu, Qiang Mao, Mei Shang, Xuerong Li, Yan Huang, Xinbing Yu
    Parasitology Research.2014; 113(9): 3409.     CrossRef
  • ClonorESTdb: a comprehensive database for Clonorchis sinensis EST sequences
    Dae-Won Kim, Won Gi Yoo, Sanghyun Lee, Myoung-Ro Lee, Yu-Jung Kim, Shin-Hyeong Cho, Won-Ja Lee, Jung-Won Ju
    BMC Research Notes.2014;[Epub]     CrossRef
  • Adult Opisthorchis felineus major protein fractions deduced from transcripts: Comparison with liver flukes Opisthorchis viverrini and Clonorchis sinensis
    Mikhail Pomaznoy, Sergey Tatkov, Alexey Katokhin, Dmitry Afonnikov, Vladimir Babenko, Dagmara Furman, Ilya Brusentsov, Pavel Belavin, Alexandr Najakshin, Sergey Guselnikov, Gennady Vasiliev, Anton Sivkov, Egor Prokhortchouk, Konstantin Skryabin, Viatchesl
    Experimental Parasitology.2013; 135(2): 297.     CrossRef
  • Biochemical characterization and functional analysis of fructose-1,6-bisphosphatase from Clonorchis sinensis
    Pei Liang, Jiufeng Sun, Yan Huang, Fan Zhang, Juanjuan Zhou, Yue Hu, Xiaoyun Wang, Chi Liang, Minghui Zheng, Yanquan Xu, Qiang Mao, Xuchu Hu, Xuerong Li, Jin Xu, Gang Lu, Xinbing Yu
    Molecular Biology Reports.2013; 40(7): 4371.     CrossRef
  • Genetic diversity of nuclear ITS1–5.8S–ITS2 rDNA sequence in Clonorchis sinensis Cobbold, 1875 (Trematoda: Opisthorchidae) from the Russian Far East
    Yulia V. Tatonova, Galina N. Chelomina, Vladimir V. Besprosvannykh
    Parasitology International.2012; 61(4): 664.     CrossRef
  • Genomics and molecular genetics of Clonorchis sinensis: Current status and perspectives
    Si-Yang Huang, Guang-Hui Zhao, Bao-Quan Fu, Min-Jun Xu, Chun-Ren Wang, Song-Ming Wu, Feng-Cai Zou, Xing-Quan Zhu
    Parasitology International.2012; 61(1): 71.     CrossRef
  • Molecular characterization of Clonorchis sinensis tetraspanin 2 extracellular loop 2
    Tae Yun Kim, Eun Joo Chung, Woon-Mok Sohn, Sung-Hong Hong, Tai-Soon Yong
    Parasitology Research.2012; 110(2): 707.     CrossRef
  • Developmental Transcriptomic Features of the Carcinogenic Liver Fluke, Clonorchis sinensis
    Won Gi Yoo, Dae-Won Kim, Jung-Won Ju, Pyo Yun Cho, Tae Im Kim, Shin-Hyeong Cho, Sang-Haeng Choi, Hong-Seog Park, Tong-Soo Kim, Sung-Jong Hong, Banchob Sripa
    PLoS Neglected Tropical Diseases.2011; 5(6): e1208.     CrossRef
  • Fish-borne Parasitic Diseases
    Jong-Yil Chai
    Hanyang Medical Reviews.2010; 30(3): 223.     CrossRef
  • 12,778 View
  • 86 Download
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Brief Communications

Partial Purification and Characterization of a Cysteine Protease Inhibitor from the Plerocercoid of Spirometra erinacei
Young-Bae Chung, Hyun-Jong Yang
Korean J Parasitol 2008;46(3):183-186.
Published online September 20, 2008
DOI: https://doi.org/10.3347/kjp.2008.46.3.183

Helminthic cysteine proteases are well known to play critical roles in tissue invasion, nutrient uptake, and immune evasion of the parasites. In the same manner, the sparganum, the plerocercoid of Spirometra mansoni, is also known to secrete a large amount of cysteine proteases. However, cysteine protease inhibitors regulating the proteolytic activities of the cysteine protease are poorly illustrated. In this regard, we partially purified an endogenous cysteine protease inhibitor from spargana and characterized its biochemical properties. The cysteine protease inhibitor was purified by sequential chromatographies using Resource Q anion exchanger and Superdex 200 HR gel filtration from crude extracts of spargana. The molecular weight of the purified protein was estimated to be about 11 kD on SDS-PAGE. It was able to inhibit papain and 27 kDa cysteine protease of spargana with the ratio of 25.7% and 49.1%, respectively, while did not inhibit chymotrypsin. This finding suggests that the cysteine protease inhibitor of spargana may be involved in regulation of endogenous cysteine proteases of the parasite, rather than interact with cysteine proteases from their hosts.

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  • Identification, molecular profiling and immune functions of cystatin M in silver pomfret (Pampus argenteus)
    Yadong Xue, Xiumei Liu, Yajun Wang, Jing Chang, Xubo Wang
    Fish & Shellfish Immunology.2024; 153: 109844.     CrossRef
  • Bioinformatics analysis and prokaryotic expression of a cystatin analogue from Spirometra erinaceieuropaei
    Lin Huang, Ling Mai, Gang Lv, Xinjun Chen
    Biotechnology & Biotechnological Equipment.2023;[Epub]     CrossRef
  • Characterization of Spirometra erinaceieuropaei Plerocercoid Cysteine Protease and Potential Application for Serodiagnosis of Sparganosis
    Li Na Liu, Zhong Quan Wang, Xi Zhang, Peng Jiang, Xin Qi, Ruo Dan Liu, Zi Fang Zhang, Jing Cui, Xiao-Nong Zhou
    PLOS Neglected Tropical Diseases.2015; 9(6): e0003807.     CrossRef
  • Analysis of Structures, Functions, and Epitopes of Cysteine Protease fromSpirometra erinaceieuropaeiSpargana
    Li Na Liu, Jing Cui, Xi Zhang, Tong Wei, Peng Jiang, Zhong Quan Wang
    BioMed Research International.2013; 2013: 1.     CrossRef
  • Differential protein expression in Spirometra erinacei according to its development in its final host
    Jae-Hwan Kim, Young Ju Kim, Woon-Mok Sohn, Young Mee Bae, Sung-Tae Hong, Min-Ho Choi
    Parasitology Research.2009; 105(6): 1549.     CrossRef
  • 8,319 View
  • 84 Download
  • Crossref

Eosinophil degranulation plays a crucial role in tissue inflammatory reactions associated with helminth parasitic infections and allergic diseases. Paragonimus westermani, a lung fluke causing human paragonimiasis, secretes a large amount of cysteine proteases, which are involved in nutrient uptake, tissue invasion, and modulation of hos's immune responses. There is, however, limited information about the response of eosinophils to direct stimulation by cysteine proteases (CP) secreted by P. westermani. In the present study, we tested whether degranulation and superoxide production from human eosinophils can be induced by stimulation of the 2 CP (27 kDa and 28 kDa) purified from excretory-secretory products (ESP) of P. westermani newly excysted metacercariae (PwNEM). A large quantity of eosinophil-derived neurotoxin (EDN) was detected in the culture supernatant when human eosinophils isolated from the peripheral blood were incubated with the purified 27 kDa CP. Furthermore, the 27 kDa CP induced superoxide anion production by eosinophils in time- and dose-dependent manners. In contrast, the purified 28 kDa CP did not induce superoxide production and degranulation. These findings suggest that the 27 kDa CP secreted by PwNEM induces superoxide production and degranulation of human eosinophils, which may be involved in eosinophil-mediated tissue inflammatory responses during the larval migration in human paragonimiasis.

Citations

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  • Massive secretions in paragonimiasis pleural effusion: a new finding concerning clinical recognition and treatment
    Yunxuan Zhang, Yimin Xie, Yarui Luo, Shuang Xiang, Wen Zhong, Na Wu, Meng Chen, Xiaojiao Zhou, Shulei Peng, Qiang Chen
    European Journal of Clinical Microbiology & Infectious Diseases.2023; 42(4): 493.     CrossRef
  • Transcriptome Analysis Reveals Possible Virulence Factors of Paragonimus proliferus
    Sheng-Hao Li, Shu-De Li, Kun-Li Wu, Jun-Yi Li, Hong-Juan Li, Wei-Qun Wang, Li-Jun Yang, Jing-Jing Xu, Guo-Ji Chang, Yan-Ling Zhang, Qiu-Hong Shu, Shan-Shan Zhuang, Zhi-Qiang Ma, Shu-Meiqi He, Min Zhu, Wen-Lin Wang, Hong-Li Huang
    Current Bioinformatics.2021; 16(2): 197.     CrossRef
  • Downregulated RPS-30 in Angiostrongylus cantonensis L5 plays a defensive role against damage due to oxidative stress
    Wei-Wei Sun, Xiu-Mei Yan, Qing Shi, Yuan-Jiao Zhang, Jun-Ting Huang, Hui-Cong Huang, Hong-Fei Shi, Bao-Long Yan
    Parasites & Vectors.2020;[Epub]     CrossRef
  • Molecular and immunological characterization of cathepsin L-like cysteine protease of Paragonimus pseudoheterotremus
    Tippayarat Yoonuan, Supaporn Nuamtanong, Paron Dekumyoy, Orawan Phuphisut, Poom Adisakwattana
    Parasitology Research.2016; 115(12): 4457.     CrossRef
  • Conservation and diversification of the transcriptomes of adult Paragonimus westermani and P. skrjabini
    Ben-wen Li, Samantha N. McNulty, Bruce A. Rosa, Rahul Tyagi, Qing Ren Zeng, Kong-zhen Gu, Gary J. Weil, Makedonka Mitreva
    Parasites & Vectors.2016;[Epub]     CrossRef
  • Systems Biology Studies of Adult Paragonimus Lung Flukes Facilitate the Identification of Immunodominant Parasite Antigens
    Samantha N. McNulty, Peter U. Fischer, R. Reid Townsend, Kurt C. Curtis, Gary J. Weil, Makedonka Mitreva, Aaron R. Jex
    PLoS Neglected Tropical Diseases.2014; 8(10): e3242.     CrossRef
  • Eosinophilic Pneumonias
    Praveen Akuthota, Peter F. Weller
    Clinical Microbiology Reviews.2012; 25(4): 649.     CrossRef
  • Eosinophil and Tissue-invasive Parasitic Helminth
    Myeong Heon Shin
    Hanyang Medical Reviews.2010; 30(3): 238.     CrossRef
  • Eosinophil-Mediated Tissue Inflammatory Responses in Helminth Infection
    Myeong Heon Shin, Young Ah Lee, Duk-Young Min
    The Korean Journal of Parasitology.2009; 47(Suppl): S125.     CrossRef
  • The global cysteine peptidase landscape in parasites
    Holly J. Atkinson, Patricia C. Babbitt, Mohammed Sajid
    Trends in Parasitology.2009; 25(12): 573.     CrossRef
  • Parasitic helminths: a pharmacopeia of anti-inflammatory molecules
    M. J. G. JOHNSTON, J. A. MacDONALD, D. M. McKAY
    Parasitology.2009; 136(2): 125.     CrossRef
  • 8,318 View
  • 75 Download
  • Crossref
Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes
Ji-Young Kim, Hyun-Jong Yang, Kwang-Sig Kim, Young-Bae Chung
Korean J Parasitol 2005;43(4):157-160.
Published online December 20, 2005
DOI: https://doi.org/10.3347/kjp.2005.43.4.157

A 29 kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required.

Citations

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  • Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis
    Ariel Naidich, Ariana M. Gutierrez, Federico Camicia
    Parasite.2024; 31: 39.     CrossRef
  • Cloning and characterization of a cathepsin L-like cysteine protease from Taenia pisiformis
    Qiuxia Wang, Shaohua Zhang, Xuenong Luo, Junling Hou, Xueliang Zhu, Xuepeng Cai
    Veterinary Parasitology.2013; 194(1): 26.     CrossRef
  • Partial Purification and Characterization of a Cysteine Protease Inhibitor from the Plerocercoid of Spirometra erinacei
    Young-Bae Chung, Hyun-Jong Yang
    The Korean Journal of Parasitology.2008; 46(3): 183.     CrossRef
  • Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes
    Yasuhito Sako, Hiroshi Yamasaki, Kazuhiro Nakaya, Minoru Nakao, Akira Ito
    Molecular and Biochemical Parasitology.2007; 154(2): 181.     CrossRef
  • Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode
    Ai Hua Li, Sung-Ung Moon, Yun-Kyu Park, Byoung-Kuk Na, Myung-Gi Hwang, Chang-Mi Oh, Shin-Hyeong Cho, Yoon Kong, Tong-Soo Kim, Pyung-Rim Chung
    Veterinary Parasitology.2006; 141(3-4): 251.     CrossRef
  • 8,140 View
  • 90 Download
  • Crossref

Original Article

Cloning and expression of trypsin-encoding cDNA from Blattella germanica and its possibility as an allergen
Mee Sun Ock, Bong Jin Kim, Sun Mi Kim, Kang Hyun Byun
Korean J Parasitol 2005;43(3):101-110.
Published online September 20, 2005
DOI: https://doi.org/10.3347/kjp.2005.43.3.101

In this study, the trypsin gene (bgtryp-1) from the German cockroach, Blattella germanica, was cloned via the immunoscreening of patients with allergies to cockroaches. Nucleotide sequence analysis predicted an 863 bp open reading frame which encodes for 257 amino acids. The deduced amino acid sequence exhibited 42-57% homology with the serine protease from dust mites, and consisted of a conserved catalytic domain (GDSGGPLV). bgtryp-1 was determined by both Northern and Southern analysis to be a 0.9 kb, single-copy gene. SDS-PAGE and Western blotting analyses of the recombinant protein (Bgtryp-1) over-expressed in Escherichia coli revealed that the molecular mass of the expressed protein was 35 kDa, and the expressed protein was capable of reacting with the sera of cockroach allergy patients. We also discussed the possibility that trypsin excreted by the digestive system of the German cockroach not only functions as an allergen, but also may perform a vital role in the activation of PAR-2.

Citations

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  • Proteinase‐activated receptor‐2 antagonist C391 inhibits Alternaria‐induced airway epithelial signalling and asthma indicators in acute exposure mouse models
    Candy M. Rivas, Michael C. Yee, Kenneth J. Addison, Marissa Lovett, Kasturi Pal, Julie G. Ledford, Gregory Dussor, Theodore J. Price, Josef Vagner, Kathryn A. DeFea, Scott Boitano
    British Journal of Pharmacology.2022; 179(10): 2208.     CrossRef
  • Insect Allergens on the Dining Table
    Kyoung Yong Jeong, Jung-Won Park
    Current Protein & Peptide Science.2020; 21(2): 159.     CrossRef
  • Protease-activated receptor-2 signaling through β-arrestin-2 mediates Alternaria alkaline serine protease-induced airway inflammation
    Michael C. Yee, Heddie L. Nichols, Danny Polley, Mahmoud Saifeddine, Kasturi Pal, Kyu Lee, Emma H. Wilson, Michael O. Daines, Morley D. Hollenberg, Scott Boitano, Kathryn A. DeFea
    American Journal of Physiology-Lung Cellular and Molecular Physiology.2018; 315(6): L1042.     CrossRef
  • Cockroach allergen serine proteinases: Isolation, sequencing and signalling via proteinase‐activated receptor‐2
    D. J. Polley, K. Mihara, R. Ramachandran, H. Vliagoftis, B. Renaux, M. Saifeddine, M. O. Daines, S. Boitano, M. D. Hollenberg
    Clinical & Experimental Allergy.2017; 47(7): 946.     CrossRef
  • Allergenic Characterization of a Novel Allergen, Homologous to Chymotrypsin, from German Cockroach
    Kyoung Yong Jeong, Mina Son, Jae-Hyun Lee, Chein-Soo Hong, Jung-Won Park
    Allergy, Asthma & Immunology Research.2015; 7(3): 283.     CrossRef
  • Characterization of Recombinant Per a 10 from Periplaneta americana
    Dhanapal Govindaraj, Shailendra Nath Gaur, Naveen Arora
    Clinical and Vaccine Immunology.2013; 20(2): 262.     CrossRef
  • Characterization of a chemostable serine alkaline protease from Periplaneta americana
    Prashant T Sanatan, Purushottam R Lomate, Ashok P Giri, Vandana K Hivrale
    BMC Biochemistry.2013;[Epub]     CrossRef
  • Household Arthropod Allergens in Korea
    Tai-Soon Yong, Kyoung Yong Jeong
    The Korean Journal of Parasitology.2009; 47(Suppl): S143.     CrossRef
  • Identification of a serine protease as a major allergen (Per a 10) of Periplaneta americana
    V. T. Sudha, N. Arora, S. N. Gaur, S. Pasha, B. P. Singh
    Allergy.2008; 63(6): 768.     CrossRef
  • Inflammatory effect of environmental proteases on airway mucosa
    Charles E. Reed
    Current Allergy and Asthma Reports.2007; 7(5): 368.     CrossRef
  • Expressed sequence tags analysis of Blattella germanica
    Hyang Suk Chung, Tai Hyun Yu, Bong Jin Kim, Sun Mi Kim, Joo Yeong Kim, Hak Sun Yu, Hae Jin Jeong, Mee Sun Ock
    The Korean Journal of Parasitology.2005; 43(4): 149.     CrossRef
  • 10,002 View
  • 66 Download
  • Crossref

Brief Communication

Degranulation of human eosinophils induced by Paragonimus westermani-secreted protease
Myeong Heon Shin, Young-Bae Chung, Hirohito Kita
Korean J Parasitol 2005;43(1):33-37.
Published online March 20, 2005
DOI: https://doi.org/10.3347/kjp.2005.43.1.33

Eosinophil degranulation is considered to be a key effector function for the killing of helminthic worms and tissue inflammation at worm-infected lesion sites. However, relatively little data are available with regard to eosinophil response after stimulation with worm-secreted products which contain a large quantity of cysteine proteases. In this study, we attempted to determine whether the degranulation of human eosinophils could be induced by the direct stimulation of the excretory-secretory products (ESP) of Paragonimus westermani, which causes pulmonary paragonimiasis in human beings. Incubation of eosinophils for 3 hr with Paragonimus-secreted products resulted in marked degranulation, as evidenced by the release of eosinophil-derived neurotoxin (EDN) in the culture supernatants. Moreover, superoxide anion was produced by eosinophils after stimulation of the ESP. The ESP-induced EDN release was found to be significantly inhibited when the ESP was pretreated with protease inhibitor cocktail or the cysteine protease inhibitor, E-64. These findings suggest that human eosinophils become degranulated in response to P. westermani-secreted proteases, which may contribute to in vivo tissue inflammation around the worms.

Citations

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  • A 27 kDa Cysteine Protease Secreted by Newly Excysted Paragonimus westermani Metacercariae Induces Superoxide Anion Production and Degranulation of Human Eosinophils
    Young-Bae Chung, Hirohito Kita, Myeong Heon Shin
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  • Identification of immunodominant excretory–secretory cysteine proteases of adult Paragonimus westermani by proteome analysis
    Eung‐Goo Lee, Byoung‐Kuk Na, Young‐An Bae, Seon‐Hee Kim, Eun‐Young Je, Jeong‐Won Ju, Shin‐Hyeong Cho, Tong‐Soo Kim, Shin‐Yong Kang, Seung‐Yull Cho, Yoon Kong
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  • Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes
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Original Articles

Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates
Byoung-Kuk Na, Eung-Goo Lee, Hyeong-Woo Lee, Shin-Hyeong Cho, Young-An Bae, Yoon Kong, Jong-Koo Lee, Tong-Soo Kim
Korean J Parasitol 2004;42(2):61-66.
Published online June 20, 2004
DOI: https://doi.org/10.3347/kjp.2004.42.2.61

The plasmepsins are the aspartic proteases of malaria parasites. Treatment of aspartic protease inhibitor inhibits hemoglobin hydrolysis and blocks the parasite development in vitro suggesting that these proteases might be exploited their potentials as antimalarial drug targets. In this study, we determined the genetic variations of the aspartic proteases of Plasmodium vivax (PvPMs) of wild isolates. Two plasmepsins (PvPM4 and PvPM5) were cloned and sequenced from 20 P. vivax Korean isolates and two imported isolates. The sequences of the enzymes were highly conserved except a small number of amino acid substitutions did not modify key residues for the function or the structure of the enzymes. The high sequence conservations between the plasmepsins from the isolates support the notion that the enzymes could be reliable targets for new antimalarial chemotherapeutics.

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Purification and characterization of a 33 kDa serine protease from Acanthamoeba lugdunensis KA/E2 isolated from a Korean keratitis patient
Hyo-Kyung Kim, Young-Ran Ha, Hak-Sun Yu, Hyun-Hee Kong, Dong-Il Chung
Korean J Parasitol 2003;41(4):189-196.
Published online December 20, 2003
DOI: https://doi.org/10.3347/kjp.2003.41.4.189

In order to evaluate the possible roles of secretory proteases in the pathogenesis of amoebic keratitis, we purified and characterized a serine protease secreted by Acanthamoeba lugdunensis KA/E2, isolated from a Korean keratitis patient. The ammonium sulfate-precipitated culture supernatant of the isolate was purified by sequential chromatography on CM-Sepharose, Sephacryl S-200, and mono Q-anion exchange column. The purified 33 kDa protease had a pH optimum of 8.5 and a temperature optimum of 55℃. Phenylmethylsulfonylfluoride and 4-(2-Aminoethyl)-benzenesulfonyl-fluoride, both serine protease specific inhibitors, inhibited almost completely the activity of the 33 kDa protease whereas other classes of inhibitors did not affect its activity. The 33 kDa enzyme degraded various extracellular matrix proteins and serum proteins. Our results strongly suggest that the 33 kDa serine protease secreted from this keratopathogenic Acanthamoeba play important roles in the pathogenesis of amoebic keratitis, such as in corneal tissue invasion, immune evasion and nutrient uptake.

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Protease activity of 80 kDa protein secreted from the apicomplexan parasite Toxoplasma gondii
Kyoung-Ju Song, Ho-Woo Nam
Korean J Parasitol 2003;41(3):165-169.
Published online September 20, 2003
DOI: https://doi.org/10.3347/kjp.2003.41.3.165

This study describes the characterization of 80 kDa protease showing gelationlytic property among three proteases in the excretory/secretory proteins (ESP) from Toxoplasma gondii. The protease activity was detected in the ESP but not in the somatic extract of RH tachyzoites. This protease was active only in the presence of calcium ion but not other divalent cationic ions such as Cu2+, Zn2+, Mg2+, and Mn2+, implying that Ca2+ is critical factor for the activation of the protease. The 80 kDa protease was optimally active at pH 7.5. Its gelatinolytic activity was maximal at 37℃, and significant level of enzyme activity of the protease remained after heat treatment at 56℃ for 30 min or 100℃ for 10 min. This thermostable enzyme was strongly inhibited by metal chelators, i.e., EDTA, EGTA, and 1,10-phenanthroline. Thus, the 80 kDa protease n the ESP secreted by T. gondii was classified as a calcium dependent neutral metalloprotease.

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Degradation of immunoglobulins, protease inhibitors, and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii
Byoung-Kuk Na, Jong-Hwa Cho, Chul-Yong Song, Tong-Soo Kim
Korean J Parasitol 2002;40(2):93-99.
Published online June 30, 2002
DOI: https://doi.org/10.3347/kjp.2002.40.2.93

The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (sIgA), IgG, and IgM. It also degraded interleukin-1α (IL-1α) and IL-1β. Its activity was not inhibited by endogenous protease inhibitors, such as α2-macroglobulin, α1-trypsin inhibitor, and α2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthamoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

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Excretory bladder: the source of cysteine proteases in Paragonimus westermani metacercariae
Hyun-Jong Yang, Young-Bae Chung, Shin-Yong Kang, Yoon Kong, Seung-Yull Cho
Korean J Parasitol 2002;40(2):89-92.
Published online June 30, 2002
DOI: https://doi.org/10.3347/kjp.2002.40.2.89

The cysteine proteases of Paragonimus westermani metacercariae are involved in metacercarial excystment, host immune modulation, and possibly in tissue penetration. In order to clarify the origin of the enzymes, 28 and 27 kDa cysteine proteases in metacercarial excretory-secretory products were purified through the FPLC system using Mono Q column chromatography. The polyclonal antibodies to the enzymes were produced in BALB/c mice. Immunolocalization studies revealed that both cysteine proteases were distributed at the linings of excretory bladder and excretory concretions of the metacercariae. It was suggested that the excretory epithelium of P. westermani undertake the secretory function of metacercarial cysteine proteases, in addition to its role as a route for eliminating waste products.

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  • Early Cysteine Protease Activity in Excretory Bladder Triggers Metacercaria Excystment of Paragonimus westermani
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Brief Communications

Differential expression of the 27 kDa cathepsin L-like cysteine protease in developmental stages of Spirometra erinacei
Yoon Kong, Doo-Hee Yun, Seung-Yull Cho, Woon-Mok Sohn, Young-Bae Chung, Shin-Yong Kang
Korean J Parasitol 2000;38(3):195-199.
Published online September 30, 2000
DOI: https://doi.org/10.3347/kjp.2000.38.3.195

The 27 kDa cathepsin L-like cysteine protease of Spirometra erinacei plerocercoid is known to play an important function in tissue penetration, nutrient uptake and immune modulation in human sparganosis. In the present study, the expression of this enzyme was examined at different developmental stages of S. erinacei including immature egg, coracidium, plerocercoid in tadpole and rat, and adult. Proteolytic activity against carboxybenzoyl-phenylalanyl-arginyl-7-amino-4-methylcoumarin was detected in the extracts of coracidia and plerocercoid while no activity was observed in those of immature egg and adult. The specific activity in coracidial extracts was lower than that in the plerocercoid. Reverse transcription-polymerase chain reaction and Northern blot analysis demonstrated that the gene was expressed in the coracidium and plerocercoid but not in immature egg and adult. These results suggest that the 27 kDa cysteine protease is only expressed in the stages involving active migration of the parasite in the host tissue.

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    Hyun Jong Yang
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Partial characterization of a 17 kDa protein of Clonorchis sinensis
Young-Bae Chung, Byung-Suk Chung, Min-Ho Choi, Jong-Yil Chai, Sung-Tae Hong
Korean J Parasitol 2000;38(2):95-97.
Published online June 30, 2000
DOI: https://doi.org/10.3347/kjp.2000.38.2.95

A 17 kDa protein from Clonorchis sinensis adults was purified by a procedure including Sephacryl S-200 HR gel filtration and Q-Sepharose anion exchange chromatography. The protein was proved to be a cysteine protease as it showed hydrolytic activity toward Cbz-Phe-Arg-AMC in the presence of dithiothreitol and was inhibited by specific inhibitors such as iodoacetic acid or trans epoxy-succinly-L-leucyl-amido(4-guanidino) butane. The polyclonal antibody raised against the protein reacted to 17 kDa proteins of trematodes such as Paragonimus westermani, Fasciola hepatica, Opisthorchis viverrini, Gymnophalloides seoi, and Metagonimus yokogawai. The antibody recognized the 17 kDa and 16 kDa cysteine proteases purified from C. sinensis, P. westermani, and G. seoi as well. These results suggest that the 17 kDa protein may be a cysteine protease commonly present in trematodes.

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  • EXPRESSION OF CYSTEINE PROTEINASE OF CLONORCHIS SINENSIS AND ITS USE IN SERODIAGNOSIS OF CLONORCHIASIS
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Original Article
A 54 kDa cysteine protease purified from the crude extract of Neodiplostomum seoulense adult worms
Min-Ho Choi, Seong-Choon Choe, Soon-Hyung Lee
Korean J Parasitol 1999;37(1):39-46.
Published online March 31, 1999
DOI: https://doi.org/10.3347/kjp.1999.37.1.39

As a preliminary study for the explanation of pathobiology of Neodiplostomum seoulense infection, a 54 kDa protease was purified from the crude extract of adult worms by sequential chromatographic methods. The crude extract was subjected to DEAE-Sepharose Fast Flow column, and protein was eluted using 25 mM Tris-HCl (pH 7.4) containing 0.05, 0.1, 0.2 and 0.4 M NaCl in stepwise elution. The 0.2 M NaCl fraction was further purified by Q-Sepharose chromatography and protein was eluted using 20 mM sodium acetate (pH 6.4) containing 0.05, 0.1, 0.2 and 0.3 M NaCl, respectively. The 0.1M NaCl fraction showed a single protein band on SDS-PAGE carried out on a 7.5-15% gradient gel. The proteolytic activities of the purified enzyme were specifically inhibited by L-trans-epoxy-succinylleucylamide (4-guanidino) butane (E-64) and iodoacetic acid. The enzyme, cysteine protease, showed the maximum proteolytic activity at pH 6.0 in 0.1 M buffer, and degraded extracellular matrix proteins such as collagen and fibronectin with different activities. It is suggested that the cysteine protease may play a role in the nutrient uptake of N. seoulense from the host intestine.

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