Parasites, Hosts and Diseases

"cysteine proteinase"

Original Articles

Protective Role of Purified Cysteine Proteinases against Fasciola gigantica Infection in Experimental Animals: Eman EL-Ahwany, Ibrahim Rabia, Faten Nagy, Mona Zoheiry, Tarek Diab, Suher Zada; Korean J Parasitol 2012;50(1):45-51.
Published online March 6, 2012; DOI: https://doi.org/10.3347/kjp.2012.50.1.45

Abstract
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Fascioliasis is one of the public health problems in the world. Cysteine proteinases (CP) released by Fasciola gigantica play a key role in parasite feeding, migration through host tissues, and in immune evasion. There has been some evidence from several parasite systems that proteinases might have potential as protective antigens against parasitic infections. Cysteine proteinases were purified and tested in vaccine trials of sheep infected with the liver fluke. Multiple doses (2 mg of CP in Freund's adjuvant followed by 3 booster doses 1 mg each at 4 week intervals) were injected intramuscularly into sheep 1 week prior to infect orally with 300 F. gigantica metacercariae. All the sheep were humanely slaughtered 12 weeks after the first immunization. Changes in the worm burden, ova count, and humoral and cellular responses were evaluated. Significant reduction was observed in the worm burden (56.9%), bile egg count (70.7%), and fecel egg count (75.2%). Immunization with CP was also found to be associated with increases of total IgG, IgG₁, and IgG₂ (P<0.05). Data showed that the serum cytokine levels of pro-inflammatory cytokines, IL-12, IFN-γ, and TNF-α, revealed significant decreases (P<0.05). However, the anti-inflammatory cytokine levels, IL-10, TGF-β, and IL-6, showed significant increases (P<0.05). In conclusion, it has been found that CP released by F. gigantica are highly important candidates for a vaccine antigen because of their role in the fluke biology and host-parasite relationships.

Citations

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Genetic diversity and adaptability of native sheep breeds from different climatic zones
George Wanjala, Zoltán Bagi, Dinu Gavojdian, Bouabid Badaoui, Putri Kusuma Astuti, Alexandru Mizeranschi, Elena Ilisiu, Husein Ohran, Eva Pasic Juhas, Dimitrios Loukovitis, Aldona Kawęcka, Rūta Šveistienė, Zsolt Becskei, Péter Strausz, Nelly Kichamu, Szil
Scientific Reports.2025;[Epub] CrossRef
Serodiagnosis of Fasciola gigantica Infection in Buffaloes with Native Cathepsin-L Proteases and Recombinant Cathepsin L1-D
Andleeb Aftab, Rohit Lall, Savita Bisen, Arun Anandanarayanan, Ajayta Rialch, Jayanta K. Chamuah, Shobha Yadav, M. Silamparasan, O. K. Raina
Acta Parasitologica.2020; 65(2): 413. CrossRef
A Survey on the Adjuvant Role of Naloxone Alone or Combined with Alum in Vaccination Against Fasciolosis in BALB/c Mice
Hakim Azizi, Hadi Mirzaeei, Amin Bagheri, Ali Bazi, Ali Khamesipour, Hajar Yaghoobi, Aliyar Mirzapour, Mehrdad Khatami, Samira Elikaee
Acta Parasitologica.2019;[Epub] CrossRef
Oral delivery of Bacillus subtilis spores expressing cysteine protease of Clonorchis sinensis to grass carp ( Ctenopharyngodon idellus ): Induces immune responses and has no damage on liver and intestine function
Zeli Tang, Hengchang Sun, TingJin Chen, Zhipeng Lin, Hongye Jiang, Xinyi Zhou, Cunbin Shi, Houjun Pan, Ouqin Chang, Pengli Ren, Jinyun Yu, Xuerong Li, Jin Xu, Yan Huang, Xinbing Yu
Fish & Shellfish Immunology.2017; 64: 287. CrossRef
Comparative analysis of immune effects in mice model: Clonorchis sinensis cysteine protease generated from recombinant Escherichia coli and Bacillus subtilis spores
Zhanshuai Wu, Zeli Tang, Mei Shang, Lu Zhao, Lina Zhou, Xiangzhan Kong, Zhipeng Lin, Hengchang Sun, Tingjin Chen, Jin Xu, Xuerong Li, Yan Huang, Xinbing Yu
Parasitology Research.2017; 116(7): 1811. CrossRef
The immunological characteristics and probiotic function of recombinant Bacillus subtilis spore expressing Clonorchis sinensis cysteine protease
Zeli Tang, Mei Shang, Tingjin Chen, Pengli Ren, Hengchang Sun, Hongling Qu, Zhipeng Lin, Lina Zhou, Jinyun Yu, Hongye Jiang, Xinyi Zhou, Xuerong Li, Yan Huang, Jin Xu, Xinbing Yu
Parasites & Vectors.2016;[Epub] CrossRef
Immunological features of LPS from Ochrobactrum intermedium on sheep experimentally infected with Fasciola hepatica
J.M. Martínez-Pérez, D. Robles-Pérez, F.A. Rojo-Vázquez, M. Martínez-Valladares
Research in Veterinary Science.2014; 97(2): 329. CrossRef
Liver fluke vaccines in ruminants: strategies, progress and future opportunities
Hayley Toet, David M. Piedrafita, Terry W. Spithill
International Journal for Parasitology.2014; 44(12): 915. CrossRef

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Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani: Joon-Hyuck Choi, Jae-Hyuk Lee, Hak-Sun Yu, Hae-Jin Jeong, Jin Kim, Yeon-Chul Hong, Hyun-Hee Kong, Dong-Il Chung; Korean J Parasitol 2006;44(3):187-196.
Published online September 20, 2006; DOI: https://doi.org/10.3347/kjp.2006.44.3.187

Abstract
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The mammalian trematode Paragonimus westermani is a typical digenetic parasite, which can cause paragonimiasis in humans. Host tissues and blood cells are important sources of nutrients for development, growth and reproduction of P. westermani. In this study, a cDNA clone encoding a 47 kDa hemoglobinase of P. westermani was characterized by sequencing analysis, and its localization was investigated immunohistochemically. The phylogenetic tree prepared based on the hemoglobinase gene showed high homology with hemoglobinases of Fasciola hepatica and Schistosoma spp. Moreover, recombinant P. westermani hemoglobinase degradaded human hemoglobin at acidic pH (from 3.0 to 5.5) and its activity was almost completely inhibited by E-64, a cysteine proteinase inhibitor. Immunohistochemical studies showed that P. westermani hemoglobinase was localized in the epithelium of the adult worm intestine implying that the protein has a specific function. These observations suggest that hemoglobinase may act as a digestive enzyme for acquisition of nutrients from host hemoglobin. Further investigations may provide insights into hemoglobin catabolism in P. westermani.

Citations

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Multi-stage transcriptome profiling of the neglected food-borne echinostome Artyfechinostomum sufrartyfex reveal potential diagnostic and drug targets
Suman Dahal, Pratibha Gour, Saurabh Raghuvanshi, Yugal Kishore Prasad, Dipshikha Saikia, Sudeep Ghatani
Acta Tropica.2022; 233: 106564. CrossRef
Characterization and localization of antigens for serodiagnosis of human paragonimiasis
Kurt C. Curtis, Kerstin Fischer, Young-Jun Choi, Makedonka Mitreva, Gary J. Weil, Peter U. Fischer
Parasitology Research.2021; 120(2): 535. CrossRef
Cysteine proteases as digestive enzymes in parasitic helminths
Conor R. Caffrey, Louise Goupil, Karina M. Rebello, John P. Dalton, David Smith, Aaron R. Jex
PLOS Neglected Tropical Diseases.2018; 12(8): e0005840. 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
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Paragonimus worm from a New Guinea native in 1926
Wenlin Wang, David Blair, Tian Min, Fang Li, Dianhua Wang
Asian Pacific Journal of Tropical Medicine.2011; 4(1): 76. CrossRef
Asparaginyl endopeptidase from the carcinogenic liver fluke, Opisthorchis viverrini, and its potential for serodiagnosis
Thewarach Laha, Jittiyawadee Sripa, Banchob Sripa, Mark Pearson, Leon Tribolet, Sasithorn Kaewkes, Paiboon Sithithaworn, Paul J. Brindley, Alex Loukas
International Journal of Infectious Diseases.2008; 12(6): e49. CrossRef

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Purification of a 68-kDa cysteine proteinase from crude extract of Pneumocystis carinii: Min-Ho Choi, Byung-Suk Chung, Young-Bae Chung, Jae-Ran Yu, Sang Rock Cho, Sung-Tae Hong; Korean J Parasitol 2000;38(3):159-166.
Published online September 30, 2000; DOI: https://doi.org/10.3347/kjp.2000.38.3.159

Abstract
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The present study intended to verify activities of cysteine proteinase of Pneumocystis carinii from rats and to purify the enzyme. In order to exclude the contamination of host-derived enzymes, concentrates of P. carinii was primarily treated with a mixture of proteinase inhibitors before lysis of P. carinii. A 68-kDa cysteine proteinase was finally purified from the crude extract of P. carinii by 4 sequential chromatographic methods. The enzyme showed an optimal activity at pH 5.5 in 0.1 M sodium acetate, and its activity was specifically inhibited by L-trans-epoxysuccinylleucylamido (4-guanidino) butane (E-64) and iodoacetic acid, suggesting that the enzyme is a cysteine proteinase. The 68-kDa proteinase weakly digested macromolecules such as collagen, hemoglobin and fibronectin. The present study demonstrated the activity of cysteine proteinase at the 68-kDa band of P. carinii, and purified and characterized the molecule.

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Comparative Genomics Suggests that the Fungal Pathogen Pneumocystis Is an Obligate Parasite Scavenging Amino Acids from Its Host's Lungs
Philippe M. Hauser, Frédéric X. Burdet, Ousmane H. Cissé, Laurent Keller, Patrick Taffé, Dominique Sanglard, Marco Pagni, Jason E. Stajich
PLoS ONE.2010; 5(12): e15152. CrossRef
Characterization of a Novel ADAM Protease Expressed byPneumocystis carinii
Cassie C. Kennedy, Theodore J. Kottom, Andrew H. Limper
Infection and Immunity.2009; 77(8): 3328. CrossRef

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Degradations of human immunoglobulins and hemoglobin by a 60 kDa cysteine proteinase of Trichomonas vaginalis: Duk-Young Min, Keun-Hee Hyun, Jae-Sook Ryu, Myoung-Hee Ahn, Myung-Hwan Cho; Korean J Parasitol 1998;36(4):261-268.
Published online December 20, 1998; DOI: https://doi.org/10.3347/kjp.1998.36.4.261

Abstract
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The present study was undertaken to investigate the role of cysteine proteinase of Trichomonas vaginalis in escaping from host defense mechanism. A cysteine proteinase of T. vaginalis was purified by affinity chromatography and gel filtration. Optimum pH for the purified proteinase activity was 6.0. The proteinase was inhibited by cysteine and serine proteinase inhibitors such as E-64, NEM, IAA, leupeptin, TPCK and TLCK, and also by Hg²⁺, but not affected by serine-, metallo-, and aspartic proteinase inhibitors such as PMSF, EDTA and pepstatin A. However, it was activated by the cysteine proteinase activator, DTT. The molecular weight of a purified proteinase was 62 kDa on gel filtration and 60 kDa on SDS-PAGE. Interestingly, the purified proteinase was able to degrade serum IgA, secretory IgA, and serum IgG in time- and dose-dependent manners. In addition, the enzyme also degraded hemoglobin in a dose-dependent manner. These results suggest that the acidic cysteine proteinase of T. vaginalis may play a dual role for parasite survival in conferring escape from host humoral defense by degradation of immunoglobulins, and in supplying nutrients to parasites by degradation of hemoglobin.

Citations

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Hemoglobin uptake and utilization by human protozoan parasites: a review
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Hilda M. Hernández, Ricardo Marcet, Jorge Sarracent
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