Parasites, Hosts and Diseases

"cysteine protease"

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

Abstract
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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.

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Original Articles

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

Abstract
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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

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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
Unraveling the interplay between unicellular parasites and bacterial biofilms: Implications for disease persistence and antibiotic resistance
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
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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
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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
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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
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Kumiko Nakada-Tsukui, Tomoyoshi Nozaki
Cells.2021; 10(11): 2975. CrossRef
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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

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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

Abstract
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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.

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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
Parasitology Research.2025;[Epub] CrossRef
Establishment of Animal Infection Model of Spirometra Mansoni and Identification of Spirometra Mansoni by Enzyme-Linked Immunosorbent Assay
Anqi Luo, Shuyu Chen, Mingye He, Xiaoruo Tan, Zhikang Li, Wei Liu, Yisong Liu
Vector-Borne and Zoonotic Diseases.2024;[Epub] CrossRef
Case Report: Moving Tumor-Like Foci Behind Refractory Epilepsy-Cerebral Sparganosis Successfully Treated by Surgery After Failure of Praziquantel Treatment
Yusi Chen, Xu Chen, Huicong Kang
Frontiers in Neurology.2022;[Epub] CrossRef
Standardization of recombinant Ancylostoma caninum cysteine protease 2 (rAcCP2) based indirect ELISA for serodiagnosis of hookworm infection in dogs
SUCHITA P UKE, RAJAT GARG, SHAFIYA IMTIAZ RAFIQI, HIRA RAM, K L KHURANA, P S BANERJEE
The Indian Journal of Animal Sciences.2018; 88(2): 153. CrossRef
Molecular Identification of Spirometra erinaceieuropaei Tapeworm in Cases of Human Sparganosis, Hong Kong
Tommy H.C. Tang, Samson S.Y. Wong, Christopher K.C. Lai, Rosana W.S. Poon, Helen S.Y. Chan, Tak Chiu Wu, Yuk-Fai Cheung, Tak-Lap Poon, Yi-Po Tsang, Wai-Lun Tang, Alan K.L. Wu
Emerging Infectious Diseases.2017; 23(4): 665. CrossRef
Serodiagnosis of sparganosis by ELISA using recombinant cysteine protease of Spirometra erinaceieuropaei spargana
Li Na Liu, Xi Zhang, Peng Jiang, Ruo Dan Liu, Jian Zhou, Rui Zhe He, Jing Cui, Zhong Quan Wang
Parasitology Research.2015; 114(2): 753. CrossRef
Human sparganosis, a neglected food borne zoonosis
Quan Liu, Ming-Wei Li, Ze-Dong Wang, Guang-Hui Zhao, Xing-Quan Zhu
The Lancet Infectious Diseases.2015; 15(10): 1226. CrossRef
Clinical Features of Pulmonary Sparganosis
Ning Li, Yi Xiang, Yun Feng, Min Li, Bei Li Gao, Qing Yun Li
The American Journal of the Medical Sciences.2015; 350(6): 436. 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
Molecular characterization of a Spirometra mansoni antigenic polypeptide gene encoding a 28.7 kDa protein
Jing Cui, Tong Wei, Li Na Liu, Xi Zhang, Xin Qi, Zi Fang Zhang, Zhong Quan Wang
Parasitology Research.2014; 113(9): 3511. CrossRef
Development of a Rapid Diagnostic Kit That Uses an Immunochromatographic Device To Detect Antibodies in Human Sparganosis
Hiroshi Yamasaki, Takeshi Nakamura, Pewpan M. Intapan, Wanchai Maleewong, Yasuyuki Morishima, Hiromu Sugiyama, Hiroyuki Matsuoka, Kaoru Kobayashi, Katsuyoshi Takayama, Yukuharu Kobayashi, P. P. Wilkins
Clinical and Vaccine Immunology.2014; 21(9): 1360. CrossRef

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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

Abstract
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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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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

Abstract
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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

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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; Korean J Parasitol 2008;46(2):95-99.
Published online June 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.2.95

Abstract
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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.

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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
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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
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M. J. G. JOHNSTON, J. A. MacDONALD, D. M. McKAY
Parasitology.2009; 136(2): 125. CrossRef

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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

Abstract
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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

8,136 View
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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

Abstract
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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.

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Interface Molecules ofAngiostrongylus cantonensis: Their Role in Parasite Survival and Modulation of Host Defenses
Alessandra L. Morassutti, Carlos Graeff-Teixeira
International Journal of Inflammation.2012; 2012: 1. CrossRef
Echinococcus multilocularis: Identification and functional characterization of cathepsin B-like peptidases from metacestode
Yasuhito Sako, Kazuhiro Nakaya, Akira Ito
Experimental Parasitology.2011; 127(3): 693. 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
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
The Korean Journal of Parasitology.2008; 46(2): 95. 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 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
PROTEOMICS.2006; 6(4): 1290. 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
The Korean Journal of Parasitology.2005; 43(4): 157. CrossRef

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Original Article

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

Abstract
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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.

Citations

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Early Cysteine Protease Activity in Excretory Bladder Triggers Metacercaria Excystment of Paragonimus westermani
Y. B. Chung, T. S. Kim, H. J. Yang
Journal of Parasitology.2005; 91(4): 953. CrossRef

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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

Abstract
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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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Surgical treatment of a patient with live intracranial sparganosis for 17 years
Jialing Hu, Kaili Liao, Xiaojin Feng, Danling Jiang, Hailin Liu, Qingcui Zheng, Hai Qiu, Fuzhou Hua, Guohai Xu, Chunhua Xu
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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

Abstract
PDF

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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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

Abstract
PDF

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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