Parasites, Hosts and Diseases

"localization"

Brief Communications

Functional Identification of a Nuclear Localization Signal of MYB2 Protein in Giardia lamblia: Juri Kim, Mee Young Shin, Soon-Jung Park; Korean J Parasitol 2020;58(6):675-679.
Published online December 29, 2020; DOI: https://doi.org/10.3347/kjp.2020.58.6.675

MYB2 protein was identified as a transcription factor that showed encystation-induced expression in Giardia lamblia. Although nuclear import is essential for the functioning of a transcription factor, an evident nuclear localization signal (NLS) of G. lamblia MYB2 (GlMYB2) has not been defined. Based on putative GlMYB2 NLSs predicted by 2 programs, a series of plasmids expressing hemagglutinin (HA)-tagged GlMYB2 from the promoter of G. lamblia glutamate dehydrogenase were constructed and transfected into Giardia trophozoites. Immunofluorescence assays using anti-HA antibodies indicated that GlMYB2 amino acid sequence #507?#530 was required for the nuclear localization of GlMYB2, and this sequence was named as NLS_GlMYB2. We further verified this finding by demonstrating the nuclear location of a protein obtained by the fusion of NLS_GlMYB2 and G. lamblia glyceraldehyde 3-phosphate dehydrogenase, a non-nuclear protein. Our data on GlMYB2 will expand our understanding on NLSs functioning in G. lamblia.

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Mlf mediates proteotoxic response via formation of cellular foci for protein folding and degradation in Giardia
Martina Vinopalová, Lenka Arbonová, Zoltán Füssy, Vít Dohnálek, Abdul Samad, Tomáš Bílý, Marie Vancová, Pavel Doležal, Carmen Faso
PLOS Pathogens.2024; 20(10): e1012617. CrossRef
Identification of target genes regulated by encystation-induced transcription factor Myb2 using knockout mutagenesis in Giardia lamblia
Juri Kim, Eun-Ah Park, Mee Young Shin, Soon-Jung Park
Parasites & Vectors.2022;[Epub] CrossRef

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Characterization of Echinostoma cinetorchis endoribonuclease, RNase H: Sung-Bin Lim, Seok Ho Cha, Seung Jegal, Hojong Jun, Seo Hye Park, Bo-Young Jeon, Jhang Ho Pak, Young Yil Bakh, Tong-Soo Kim, Hyeong-Woo Lee; Korean J Parasitol 2017;55(4):451-455.
Published online August 31, 2017; DOI: https://doi.org/10.3347/kjp.2017.55.4.451

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Echinostoma cinetorchis is an oriental intestinal fluke causing significant pathological damage to the small intestine. The aim of this study was to determine a full-length cDNA sequence of E. cinetorchis endoribonuclease (RNase H; EcRNH) and to elucidate its molecular biological characters. EcRNH consisted of 308 amino acids and showed low similarity to endoribonucleases of other parasites (<40%). EcRNH had an active site centered on a putative DDEED motif instead of DEDD conserved in other species. A recombinant EcRNH produced as a soluble form in Escherichia coli showed enzymatic activity to cleave the 3'-O-P bond of RNA in a DNA-RNA duplex, producing 3'-hydroxyl and 5'-phosphate. These findings may contribute to develop antisense oligonucleotides which could damage echinostomes and other flukes.

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Molecular Characterization of Trypanosoma cruzi Tc8.2 Gene Indicates Two Differential Locations for the Encoded Protein in Epimastigote and Trypomastigote Forms: Danielle Kian, C?sar Armando Contreras Lancheros, Igor Alexandre Campos Damiani, Tamiris Zanforlin Olmos Fernandes, Phileno Pinge-Filho, M?rcia Regina Machado dos Santos, Jos? Franco da Silveira, Celso Vataru Nakamura, Jo?o Santana da Silva, Sueli Fumie Yamada-Ogatta, Lucy Megumi Yamauchi; Korean J Parasitol 2015;53(4):483-488.
Published online August 25, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.4.483

Abstract
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This report describes the molecular characterization of the Tc8.2 gene of Trypanosoma cruzi. Both the Tc8.2 gene and its encoded protein were analyzed by bioinformatics, while Northern blot and RT-PCR were used for the transcripts. Besides, immunolocalization of recombinant protein was done by immunofluorescence and electron microscopy. Analysis indicated the presence of a single copy of Tc8.2 in the T. cruzi genome and 2-different sized transcripts in epimastigotes/amastigotes and trypomastigotes. Immunoblotting showed 70 and 80 kDa polypeptides in epimastigotes and trypomastigotes, respectively, and a differential pattern of immunolocalization. Overall, the results suggest that Tc8.2 is differentially expressed during the T. cruzi life cycle.

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Original Articles

Sequence Analysis and Molecular Characterization of Wnt4 Gene in Metacestodes of Taenia solium: Junling Hou, Xuenong Luo, Shuai Wang, Cai Yin, Shaohua Zhang, Xueliang Zhu, Yongxi Dou, Xuepeng Cai; Korean J Parasitol 2014;52(2):163-168.
Published online April 18, 2014; DOI: https://doi.org/10.3347/kjp.2014.52.2.163

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Wnt proteins are a family of secreted glycoproteins that are evolutionarily conserved and considered to be involved in extensive developmental processes in metazoan organisms. The characterization of wnt genes may improve understanding the parasite's development. In the present study, a wnt4 gene encoding 491amino acids was amplified from cDNA of metacestodes of Taenia solium using reverse transcription PCR (RT-PCR). Bioinformatics tools were used for sequence analysis. The conserved domain of the wnt gene family was predicted. The expression profile of Wnt4 was investigated using real-time PCR. Wnt4 expression was found to be dramatically increased in scolex evaginated cysticerci when compared to invaginated cysticerci. In situ hybridization showed that wnt4 gene was distributed in the posterior end of the worm along the primary body axis in evaginated cysticerci. These findings indicated that wnt4 may take part in the process of cysticerci evagination and play a role in scolex/bladder development of cysticerci of T. solium.

Citations

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Transcriptome of Taenia solium during in vitro cyst activation and initial growth into the tapeworm stage
David Castaneda-Carpio, Renzo Gutierrez-Loli, Jose Maravi-Jaime, Segundo W. Del Aguila, Valeria Villar-Davila, Luz M. Moyano, Rafael Tapia-Limonchi, Stella M. Chenet, Cristina Guerra-Giraldez
Scientific Data.2025;[Epub] CrossRef
The significant sex-biased expression pattern of Sp-Wnt4 provides novel insights into the ovarian development of mud crab (Scylla Paramamosain)
Ardavan Farhadi, Shaobin Fang, Yin Zhang, Wenxiao Cui, Huan Fang, Mhd Ikhwanuddin, Hongyu Ma
International Journal of Biological Macromolecules.2021; 183: 490. CrossRef
Transcriptomic profile of two developmental stages of the cestode parasite Mesocestoides corti
T. Basika, G.P. Paludo, F.M. Araujo, A.C. Salim, F. Pais, L. Maldonado, N. Macchiaroli, J. Camargo de Lima, M. Rosenzvit, G.C. Oliveira, L. Kamenetzky, H.B. Ferreira
Molecular and Biochemical Parasitology.2019; 229: 35. CrossRef
Comparative Transcriptomic Analysis of the Larval and Adult Stages of Taenia pisiformis
Shaohua Zhang
Genes.2019; 10(7): 507. CrossRef
Molecular and biochemical characterization of Taenia solium α-enolase
Shaohua Zhang, Yanan You, Xuenong Luo, Yadong Zheng, Xuepeng Cai
Veterinary Parasitology.2018; 254: 36. CrossRef
Transcriptomic analysis of the larva Taenia multiceps
W.H. Li, N.Z. Zhang, L. Yue, Y. Yang, L. Li, H.B. Yan, T.T. Li, Z.G. Qu, W.Z. Jia, B.Q. Fu
Research in Veterinary Science.2017; 115: 407. CrossRef

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Nucleolar translocalization of GRA10 of Toxoplasma gondii transfectionally expressed in HeLa cells: Hye-Jin Ahn, Sehra Kim, Ho-Woo Nam; Korean J Parasitol 2007;45(3):165-174.
Published online September 20, 2007; DOI: https://doi.org/10.3347/kjp.2007.45.3.165

Abstract
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Toxoplasma gondii GRA10 expressed as a GFP-GRA10 fusion protein in HeLa cells moved to the nucleoli within the nucleus rapidly and entirely. GRA10 was concentrated specifically in the dense fibrillar component of the nucleolus morphologically by the overlap of GFP-GRA10 transfection image with IFA images by monoclonal antibodies against GRA10 (Tg378), B23 (nucleophosmin) and C23 (nucleolin). The nucleolar translocalization of GRA10 was caused by a putative nucleolar localizing sequence (NoLS) of GRA10. Interaction of GRA10 with TATA-binding protein associated factor 1B (TAF1B) in the yeast two-hybrid technique was confirmed by GST pull-down assay and immunoprecipitation assay. GRA10 and TAF1B were also co-localized in the nucleolus after co-transfection. The nucleolar condensation of GRA10 was affected by actinomycin D. Expressed GFP-GRA10 was evenly distributed over the nucleoplasm and the nucleolar locations remained as hollows in the nucleoplasm under a low dose of actinomycin D. Nucleolar localizing and interacting of GRA10 with TAF1B suggested the participation of GRA10 in rRNA synthesis of host cells to favor the parasitism of T. gondii.

Citations

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Intracellular life of protozoan Toxoplasma gondii: Parasitophorous vacuole establishment and survival strategies
JULIANA A. PORTES, ROSSIANE C. VOMMARO, LUCIO AYRES CALDAS, ERICA S. MARTINS-DUARTE
BIOCELL.2023; 47(4): 929. CrossRef
An in silico pipeline to filter the Toxoplasma gondii proteome for proteins that could traffic to the host cell nucleus and influence host cell epigenetic regulation
Genevieve Syn, Jenefer M Blackwell, Sarra E Jamieson, Richard W Francis
Memórias do Instituto Oswaldo Cruz.2018;[Epub] CrossRef
A novel dense granule protein NcGRA23 in Neospora caninum
Weirong Wang, Pengtao Gong, Pu Wang, Jingquan Dong, Xiaocen Wang, Zhengtao Yang, Jianhua Li, Xichen Zhang
Acta Biochimica et Biophysica Sinica.2018; 50(7): 727. CrossRef
How pathogens use linear motifs to perturb host cell networks
Allegra Via, Bora Uyar, Christine Brun, Andreas Zanzoni
Trends in Biochemical Sciences.2015; 40(1): 36. CrossRef
GRA 14, a novel dense granule protein from Neospora caninum
Gongzhen Liu, Xia Cui, Pan Hao, Daoyu Yang, Jing Liu, Qun Liu
Acta Biochimica et Biophysica Sinica.2013; 45(7): 607. CrossRef
Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21
Yuya Hirai, Emilie Louvet, Toshiyuki Oda, Masahiro Kumeta, Yuzo Watanabe, Tsuneyoshi Horigome, Kunio Takeyasu
Genes to Cells.2013; 18(9): 780. CrossRef
A Genome-Wide siRNA Screen to Identify Host Factors Necessary for Growth of the Parasite Toxoplasma gondii
Lindsey A. Moser, Angela M. Pollard, Laura J. Knoll, Mohamed Ali Hakimi
PLoS ONE.2013; 8(6): e68129. CrossRef
GRA Proteins of Toxoplasma gondii: Maintenance of Host-Parasite Interactions across the Parasitophorous Vacuolar Membrane
Ho-Woo Nam
The Korean Journal of Parasitology.2009; 47(Suppl): S29. CrossRef
Neurological and behavioral abnormalities, ventricular dilatation, altered cellular functions, inflammation, and neuronal injury in brains of mice due to common, persistent, parasitic infection
Gretchen Hermes, James W Ajioka, Krystyna A Kelly, Ernest Mui, Fiona Roberts, Kristen Kasza, Thomas Mayr, Michael J Kirisits, Robert Wollmann, David JP Ferguson, Craig W Roberts, Jong-Hee Hwang, Toria Trendler, Richard P Kennan, Yasuhiro Suzuki, Catherine
Journal of Neuroinflammation.2008;[Epub] CrossRef

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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

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.

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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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Antigenic profile and localization of Clonorchis sinensis proteins in the course of infection: Sung-Jong Hong, Tae Yun Kim, Kye-Yong Song, Woon-Mok Sohn, Shin-Yong Kang; Korean J Parasitol 2001;39(4):307-312.
Published online December 31, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.4.307

Abstract
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In the course of Clonorchis sinensis infection, antigens presented to the hosts may be in a close relation to growth of the fluke. The antigenic proteins stimulating IgG antibody production were chronologically identified by immunoblot and localized by immunohistochemical staining. In the early stage of infection until 12 weeks post-infection (PI), antigens were proteins with molecular mass larger than 34 kDa which were derived from the tegument, testes and intrauterine eggs. After 20 weeks PI, antigens recognized were 29, 27 and 26 kDa proteins from the intestine, excretory bladder and reproductive organs. It is suggested that the tegumental proteins are the most potent antigens and the excretory-secretory proteins with middle molecular mass of 26-45 kDa contribute to the high level production of antibodies after 20 weeks of the C. sinensis infection.

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Development of a multi-functional multi-probe atomic force microscope system with optical beam deflection method
Peng Li, Yongjian Shao, Ke Xu, Xiaohui Qiu
Review of Scientific Instruments.2021;[Epub] CrossRef
Identification of Myoferlin, a Potential Serodiagnostic Antigen of Clonorchiasis, via Immunoproteomic Analysis of Sera From Different Infection Periods and Excretory-Secretory Products of Clonorchis sinensis
Xiao-Xiao Ma, Yang-Yuan Qiu, Zhi-Guang Chang, Jun-Feng Gao, Rui-Ruo Jiang, Chun-Lin Li, Chun-Ren Wang, Qiao-Cheng Chang
Frontiers in Cellular and Infection Microbiology.2021;[Epub] CrossRef
Mapping of the putative epitope domain of Clonorchis sinensis paramyosin (CsPmy) recognized by CsPmy-specific immunoglobulin G in sera of human clonorchiasis
Jung-Mi Kang, Hye-Lim Ju, Jinyoung Lee, Tae Im Kim, Shin-Hyeong Cho, Tong-Soo Kim, Woon-Mok Sohn, Byoung-Kuk Na
Molecular and Biochemical Parasitology.2015; 201(1): 66. CrossRef
Coproantigen capture ELISA for detection of Clonorchis sinensis infection in experimentally infected rats
S.M. Mazidur Rahman, Min-Ho Choi, Young Mee Bae, Sung-Tae Hong
Parasitology International.2012; 61(1): 203. CrossRef
Functional Genes and Proteins of Clonorchis sinensis
Tae Im Kim, Byoung-Kuk Na, Sung-Jong Hong
The Korean Journal of Parasitology.2009; 47(Suppl): S59. CrossRef
Identification of a serodiagnostic antigen, legumain, by immunoproteomic analysis of excretory‐secretory products of Clonorchis sinensis adult worms
Jung‐Won Ju, Hyun‐Na Joo, Myoung‐Ro Lee, Shin‐Hyeong Cho, Hyeng‐Il Cheun, Jung‐Yeon Kim, Young‐Hee Lee, Kwang‐Jun Lee, Woon‐Mok Sohn, Dong‐Min Kim, Il‐Chul Kim, Byoung Chul Park, Tong‐Soo Kim
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A novel tegumental protein 31.8 kDa of Clonorchis sinensis: sequence analysis, expression, and immunolocalization
Yan Huang, Zhenwen Zhou, Xuchu Hu, Quande Wei, Jin Xu, Zhongdao Wu, Xinbing Yu
Parasitology Research.2007; 102(1): 77. CrossRef
Organ-specific antigens of Clonorchis sinensis
Shunyu Li, Byung-Suk Chung, Min-Ho Choi, Sung-Tae Hong
The Korean Journal of Parasitology.2004; 42(4): 169. CrossRef
Clinical and epidemiological data of patients with clonorchiasis
Ke-Xia Wang, Rong-Bo Zhang, Yu-Bao Cui, Ye Tian, Ru Cai, Chao-Pin Li
World Journal of Gastroenterology.2004; 10(3): 446. CrossRef
Use of a recombinant Clonorchis sinensis pore-forming peptide, clonorin, for serological diagnosis of clonorchiasis
Ji-Yun Lee, Tae Yun Kim, Xiao-Xian Gan, Shin-Yong Kang, Sung-Jong Hong
Parasitology International.2003; 52(2): 175. CrossRef