Parasites, Hosts and Diseases

"proteinase"

Original Article

Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells: Juan-Hua Quan, In-Wook Choi, Jung-Bo Yang, Wei Zhou, Guang-Ho Cha, Yu Zhou, Jae-Sook Ryu, Young-Ha Lee; Korean J Parasitol 2014;52(6):595-603.
Published online December 23, 2014; DOI: https://doi.org/10.3347/kjp.2014.52.6.595

Abstract
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Trichomonas vaginalis secretes a number of proteases which are suspected to be the cause of pathogenesis; however, little is understood how they manipulate host cells. The mammalian target of rapamycin (mTOR) regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, and transcription. We detected various types of metalloproteinases including GP63 protein from T. vaginalis trophozoites, and T. vaginalis GP63 metalloproteinase was confirmed by sequencing and western blot. When SiHa cells were stimulated with live T. vaginalis, T. vaginalis excretory-secretory products (ESP) or T. vaginalis lysate, live T. vaginalis and T. vaginalis ESP induced the mTOR cleavage in both time- and parasite load-dependent manner, but T. vaginalis lysate did not. Pretreatment of T. vaginalis with a metalloproteinase inhibitor, 1,10-phenanthroline, completely disappeared the mTOR cleavage in SiHa cells. Collectively, T. vaginalis metallopeptidase induces host cell mTOR cleavage, which may be related to survival of the parasite.

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Chromatin accessibility and gene expression in the parasite Trichomonas vaginalis
Agustina Prat, Daniela Muñoz, Ayelen Lizarraga, Julieta Seifert-Gorzycki, Estefania Sanchez-Vazquez, Patricia J. Johnson, Pablo H. Strobl-Mazzulla, Natalia de Miguel
BMC Infectious Diseases.2025;[Epub] CrossRef
Metallopeptidases as Key Virulence Attributes of Clinically Relevant Protozoa: New Discoveries, Perspectives, and Frontiers of Knowledge
Graziela Vargas Rigo, Fernanda Gomes Cardoso, Giulia Bongiorni Galego, Deisiane Fernanda da Rosa, André Luis Souza dos Santos, Tiana Tasca
Current Protein & Peptide Science.2023; 24(4): 307. CrossRef
VPS32, a member of the ESCRT complex, modulates adherence to host cells in the parasite Trichomonas vaginalis by affecting biogenesis and cargo sorting of released extracellular vesicles
Nehuén Salas, Veronica M. Coceres, Tuanne dos Santos Melo, Antonio Pereira-Neves, Vanina G. Maguire, Tania M. Rodriguez, Bruna Sabatke, Marcel I. Ramirez, Jihui Sha, James A. Wohlschlegel, Natalia de Miguel
Cellular and Molecular Life Sciences.2022;[Epub] CrossRef
Adherent Bacteria and Parasiticidal Secretion Products of Human Cervicovaginal Microbiota-Associated Lactobacillus gasseri Confer Non-Identical Cell Protection against Trichomonas vaginalis-Induced Cell Detachment
Bénédicte Pradines, Séverine Domenichini, Vanessa Lievin-Le Moal
Pharmaceuticals.2022; 15(11): 1350. CrossRef
The 50 kDa metalloproteinase TvMP50 is a zinc-mediated Trichomonas vaginalis virulence factor
Jonathan Puente-Rivera, José Luis Villalpando, Alma Villalobos-Osnaya, Laura Isabel Vázquez-Carrillo, Gloria León-Ávila, María Dolores Ponce-Regalado, César López-Camarillo, Jose Miguel Elizalde-Contreras, Eliel Ruiz-May, Rossana Arroyo, María Elizbeth Al
Molecular and Biochemical Parasitology.2017; 217: 32. CrossRef
Regulation of exosomes released from normal ovarian epithelial cells and ovarian cancer cells
Wei Zhang, Jiaxin Yang, Dongyan Cao, Yan You, Keng Shen, Peng Peng
Tumor Biology.2016; 37(12): 15763. CrossRef
Involvement of PI3K/AKT and MAPK Pathways for TNF-α Production in SiHa Cervical Mucosal Epithelial Cells Infected with <i>Trichomonas vaginalis</i>
Jung-Bo Yang, Juan-Hua Quan, Ye-Eun Kim, Yun-Ee Rhee, Byung-Hyun Kang, In-Wook Choi, Guang-Ho Cha, Jae-Min Yuk, Young-Ha Lee
The Korean Journal of Parasitology.2015; 53(4): 371. CrossRef

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Brief Communication

A Recombinant Matrix Metalloproteinase Protein from Gnathostoma spinigerum for Serodiagnosis of Neurognathostomiasis: Penchom Janwan, Pewpan M. Intapan, Hiroshi Yamasaki, Porntip Laummaunwai, Kittisak Sawanyawisuth, Chaisiri Wongkham, Chatchai Tayapiwatana, Amnat Kitkhuandee, Viraphong Lulitanond, Yukifumi Nawa, Wanchai Maleewong; Korean J Parasitol 2013;51(6):751-754.
Published online December 31, 2013; DOI: https://doi.org/10.3347/kjp.2013.51.6.751

Abstract
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Neurognathostomiasis is a severe form of human gnathostomiasis which can lead to disease and death. Diagnosis of neurognathostomiasis is made presumptively by using clinical manifestations. Immunoblotting, which recognizes antigenic components of molecular mass 21 kDa and 24 kDa in larval extracts of Gnathostoma spinigerum (Gs 21/24), has high sensitivity and specificity for diagnosis of neurognathostomiasis. However, only very small amounts of the Gs 21/24 antigens can be prepared from parasites harvested from natural or experimental animals. To overcome this problem, we recently produced a recombinant matrix metalloproteinase (rMMP) protein from G. spinigerum. In this study, we evaluated this rMMP alongside the Gs 21/24 antigens for serodiagnosis of human neurognathostomiasis. We studied sera from 40 patients from Srinagarind Hospital, Khon Kaen University, Thailand, with clinical criteria consistent with those of neurognathostomiasis, and sera from 30 healthy control adults from Thailand. All sera were tested for specific IgG antibodies against both G. spinigerum crude larval extract and rMMP protein using immunoblot analysis. The sensitivity and specificity for both antigenic preparations were all 100%. These results show that G. spinigerum rMMP protein can be used as an alternative diagnostic antigen, in place of larval extract, for serodiagnosis of neurognathostomiasis.

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Scientific Reports.2022;[Epub] CrossRef
Development of Immunochromatographic Test Kit for Rapid Detection of Specific IgG4 Antibody in Whole-Blood Samples for Diagnosis of Human Gnathostomiasis
Penchom Janwan, Pewpan M. Intapan, Lakkhana Sadaow, Rutchanee Rodpai, Hiroshi Yamasaki, Patcharaporn Boonroumkaew, Oranuch Sanpool, Tongjit Thanchomnang, Phuangphaka Sadee, Wanchai Maleewong
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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.

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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
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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
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Immunological features of LPS from Ochrobactrum intermedium on sheep experimentally infected with Fasciola hepatica
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Microarray Analysis of Differentially Expressed Genes between Cysts and Trophozoites of Acanthamoeba castellanii: Eun-Kyung Moon, Ying-Hua Xuan, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong; Korean J Parasitol 2011;49(4):341-347.
Published online December 16, 2011; DOI: https://doi.org/10.3347/kjp.2011.49.4.341

Abstract
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Acanthamoeba infection is difficult to treat because of the resistance property of Acanthamoeba cyst against the host immune system, diverse antibiotics, and therapeutic agents. To identify encystation mediating factors of Acanthamoeba, we compared the transcription profile between cysts and trophozoites using microarray analysis. The DNA chip was composed of 12,544 genes based on expressed sequence tag (EST) from an Acanthamoeba ESTs database (DB) constructed in our laboratory, genetic information of Acanthamoeba from TBest DB, and all of Acanthamoeba related genes registered in the NCBI. Microarray analysis indicated that 701 genes showed higher expression than 2 folds in cysts than in trophozoites, and 859 genes were less expressed in cysts than in trophozoites. The results of real-time PCR analysis of randomly selected 9 genes of which expression was increased during cyst formation were coincided well with the microarray results. Eukaryotic orthologous groups (KOG) analysis showed an increment in T article (signal transduction mechanisms) and O article (posttranslational modification, protein turnover, and chaperones) whereas significant decrement of C article (energy production and conversion) during cyst formation. Especially, cystein proteinases showed high expression changes (282 folds) with significant increases in real-time PCR, suggesting a pivotal role of this proteinase in the cyst formation of Acanthamoeba. The present study provides important clues for the identification and characterization of encystation mediating factors of Acanthamoeba.

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Seunghyeok Bang, So-Young Joo, Ja Moon Aung, Je Chul Lee, Byoung-Kuk Na, Yeonchul Hong, Minsang Shin
Acta Tropica.2025; 271: 107837. CrossRef
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Shin Ae Kang, Hak Sun Yu
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Behroz Mahdavi Poor, Jalil Rashedi, Vahid Asgharzadeh, Amirali Mirmazhary, Nazila Gheitarani
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mRNA Sequencing Reveals Upregulation of Glutathione S-Transferase Genes during Acanthamoeba Encystation
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Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence: Won-Tae Kim, Hyun-Hee Kong, Young-Ran Ha, Yeon-Chul Hong, Hae Jin Jeong, Hak Sun Yu, Dong-Il Chung; Korean J Parasitol 2006;44(4):321-330.
Published online December 20, 2006; DOI: https://doi.org/10.3347/kjp.2006.44.4.321

Abstract
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The pathogenic mechanism of granulomatous amebic encephalitis (GAE) and amebic keratitis (AK) by Acanthamoeba has yet to be clarified. Protease has been recognized to play an important role in the pathogenesis of GAE and AK. In the present study, we have compared specific activity and cytopathic effects (CPE) of purified 33 kDa serine proteinases from Acanthamoeba strains with different degree of virulence (A. healyi OC-3A, A. lugdunensis KA/E2, and A. castellanii Neff). Trophozoites of the 3 strains revealed different degrees of CPE on human corneal epithelial (HCE) cells. The effect was remarkably reduced by adding phenylmethylsulfonylfluoride (PMSF), a serine proteinase inhibitor. This result indicated that PMSF-susceptible proteinase is the main component causing cytopathy to HCE cells by Acanthamoeba. The purified 33 kDa serine proteinase showed strong activity toward HCE cells and extracellular matrix proteins. The purified proteinase from OC-3A, the most virulent strain, demonstrated the highest enzyme activity compared to KA/E2, an ocular isolate, and Neff, a soil isolate. Polyclonal antibodies against the purified 33 kDa serine proteinase inhibit almost completely the proteolytic activity of culture supernatant of Acanthamoeba. In line with these results, the 33 kDa serine proteinase is suggested to play an important role in pathogenesis and to be the main component of virulence factor of Acanthamoeba.

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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.

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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
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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.

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Recent Advances in Biology, Host and Microbe Interactions of the Human Sexually Transmitted Parasite Trichomonas vaginalis
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Shelley Kummer, Gary R. Hayes, Robert O. Gilbert, David H. Beach, John J. Lucas, Bibhuti N. Singh
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Biological and biochemical modulation of Trichomonas vaginalis KT9 isolate after shifting of culture medium from TPS-1 into TYM: Jae-Sook Ryu, Ryung Choi, So-Young Park, Hyun Park, Duk-Young Min; Korean J Parasitol 1998;36(4):255-260.
Published online December 20, 1998; DOI: https://doi.org/10.3347/kjp.1998.36.4.255

Abstract
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To evaluate the biological and biochemical characteristics of Trichomonas vaginalis KT9 isolate, the growth and size of trichomonads, pathogenicity in mouse, protein profiles and proteinase activity were examined after shifting the medium from TPS-1 into TYM. Generation time of trichomonads in TYM medium was 4.5 hr in comparison to TPS-1 with 7.1 hr. Size of trichomonads cultured in TPS-1 medium (8.5 ± 0.9 × 6.0 ± 0.9 ?m) was significantly smaller than those in TYM medium (10.9 ± 1.4 × 8.2 ± 0.9 ?m). Trichomonads cultured in TYM medium produced subcutaneous abscess in 9 out of 10 mice, whereas those in TPS-1 medium produced abscesses in 2 out of 10 mice. In SDS-PAGE, trichomonad lysates from both media showed ten common bands. However, trichomonads in TYM medium showed additional bands of 136 kDa, 116 kDa and 40 kDa in comparison to those in TPS-1 with 100 kDa. By immunoblot with T. vaginalis-immunized rabbit sera, T. vaginalis cultivated in both TYM and TPS-1 media showed 5 common bands, and unique bands of 116 kDa, 105 kDa, and 86 kDa were observed in trichomonads in TYM while a 140 kDa band in those in TPS-1. In gelatin SDS-PAGE, trichomonads in TYM degraded gelatin stronger than those in TPS-1. Also protease activity of trichomonads in TYM was significantly higher than that of trichomonads in TPS-1 using Bz-Pro-Phe-Arg-Nan as a substrate. According to the results, it is assumed that the shift from TPS-1 into TYM medium for cultivation of T. vaginalis might modulate the biological and biochemical properties of T. vaginalis in vitro.

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