Parasites, Hosts and Diseases

"Kyoung-Ju Song"

Brief Communications

Calpains are Involved in Entamoeba histolytica-Induced Death of HT-29 Colonic Epithelial Cells: Yun Soo Jang, Kyoung-Ju Song, Ju Young Kim, Young Ah Lee, Kyeong Ah Kim, Sang Kyou Lee, Myeong Heon Shin; Korean J Parasitol 2011;49(2):177-180.
Published online June 14, 2011; DOI: https://doi.org/10.3347/kjp.2011.49.2.177

Abstract
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Entamoeba histolytica is an enteric tissue-invading protozoan parasite that can cause amebic colitis and liver abscess in humans. E. histolytica has the capability to kill colon epithelial cells in vitro; however, information regarding the role of calpain in colon cell death induced by ameba is limited. In this study, we investigated whether calpains are involved in the E. histolytica-induced cell death of HT-29 colonic epithelial cells. When HT-29 cells were co-incubated with E. histolytica, the propidium iodide stained dead cells markedly increased compared to that in HT-29 cells incubated with medium alone. This pro-death effect induced by ameba was effectively blocked by pretreatment of HT-29 cells with the calpain inhibitor, calpeptin. Moreover, knockdown of m- and ?-calpain by siRNA significantly reduced E. histolytica-induced HT-29 cell death. These results suggest that m- and ?-calpain may be involved in colon epithelial cell death induced by E. histolytica.

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Involvement of NOX2-derived ROS in human hepatoma HepG2 cell death induced by Entamoeba histolytica
Young Ah Lee, Myeong Heon Shin
Parasites, Hosts and Diseases.2023; 61(4): 388. CrossRef
Signaling Role of NADPH Oxidases in ROS-Dependent Host Cell Death Induced by Pathogenic Entamoeba histolytica
Young Ah Lee, Seobo Sim, Kyeong Ah Kim, Myeong Heon Shin
The Korean Journal of Parasitology.2022; 60(3): 155. CrossRef
Infection Strategies of Intestinal Parasite Pathogens and Host Cell Responses
Bruno M. Di Genova, Renata R. Tonelli
Frontiers in Microbiology.2016;[Epub] CrossRef
Degradation of the Transcription Factors NF-κB, STAT3, and STAT5 Is Involved in Entamoeba histolytica-Induced Cell Death in Caco-2 Colonic Epithelial Cells
Kyeong Ah Kim, Arim Min, Young Ah Lee, Myeong Heon Shin
The Korean Journal of Parasitology.2014; 52(5): 459. CrossRef
Entamoeba histolytica Induces Cell Death of HT29 Colonic Epithelial Cells via NOX1-Derived ROS
Kyeong Ah Kim, Ju Young Kim, Young Ah Lee, Arim Min, Young Yil Bahk, Myeong Heon Shin
The Korean Journal of Parasitology.2013; 51(1): 61. CrossRef
Mechanisms of Adherence, Cytotoxicity and Phagocytosis Modulate the Pathogenesis of Entamoeba Histolytica
Nathaniel CV Christy, William A Petri
Future Microbiology.2011; 6(12): 1501. CrossRef

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Evaluation of α-Tubulin as an Antigenic and Molecular Probe to Detect Giardia lamblia: Juri Kim, Myeong Heon Shin, Kyoung-Ju Song, Soon-Jung Park; Korean J Parasitol 2009;47(3):287-291.
Published online August 28, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.3.287

Abstract
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The α/β-tubulin heterodimer is the basic subunit of microtubules in eukaryotes. Polyclonal antibodies specific to recombinant α-tubulin of Giardia lamblia were made, and found effective as a probe to specifically detect G. lamblia by immunofluorescence assays. Nucleotide sequences of α-tubulin genes were compared between G. lamblia WB and GS strains, prototypes of assemblage A and assemblage B, respectively. A set of primers was designed and used to amplify a portion of the α-tubulin gene from G. lamblia. PCR-RFLP analysis of this α-tubulin PCR product successfully differentiated G. lamblia into 2 distinct groups, assemblages A and B. The results indicate that α-tubulin can be used as a molecular probe to detect G. lamblia.

Citations

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Infection, Genetics and Evolution.2023; 113: 105482. CrossRef
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José Roberto Vargas-Villanueva, Filiberto Gutiérrez-Gutiérrez, Mariana Garza-Ontiveros, Sendar Daniel Nery-Flores, Lizeth Guadalupe Campos-Múzquiz, Dagoberto Vazquez-Obregón, Raul Rodriguez-Herrera, Lissethe Palomo-Ligas
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Juri Kim, Hye‐Yeon Lee, Kyu‐Ho Lee, Soon‐Jung Park
Journal of Eukaryotic Microbiology.2017; 64(4): 464. CrossRef
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G. Lopez‐Romero, J. Quintero, H. Astiazarán‐García, C. Velazquez
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Characterization of Microtubule-Binding and Dimerization Activity of Giardia lamblia End-Binding 1 Protein
Juri Kim, Sara Nagami, Kyu-Ho Lee, Soon-Jung Park, Ira J. Blader
PLoS ONE.2014; 9(5): e97850. CrossRef
Zoonotic potential of Giardia
Una Ryan, Simone M. Cacciò
International Journal for Parasitology.2013; 43(12-13): 943. CrossRef
Identification of Antigenic Proteins in Trichomonas vaginalis
Hye-Yeon Lee, Sujin Hyung, Jong Woong Lee, Juri Kim, Myeong Heon Shin, Jae-Sook Ryu, Soon-Jung Park
The Korean Journal of Parasitology.2011; 49(1): 79. CrossRef

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115 Download
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Seroprevalence of toxoplasmosis in Korean pregnant women: Kyoung-Ju Song, Jong-Chul Shin, Ho-Joon Shin, Ho-Woo Nam; Korean J Parasitol 2005;43(2):69-71.
Published online June 20, 2005; DOI: https://doi.org/10.3347/kjp.2005.43.2.69

Abstract
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This study was performed in order to evaluate the sero-epidemiological status of toxoplasmosis in pregnant Korean women. Among 5,175 sera and 750 amniotic fluid samples obtained from pregnant women, 41 serum samples (0.79%) and 10 (1.33%) amniotic fluid samples tested positive for IgG antibodies by ELISA. Fifty one cases showing a score more than 0.25 on ELISA were tested for PCR reaction against the SAG1 gene. Only one case of the 51 ELISA positive cases exhibited a positive reaction on all tests. This case had a history of acute nephropyelitis during early pregnancy, but fortunately, had delivered a phenotypically healthy baby. In this study, the seroprevalence of toxoplasmosis in pregnant women was found to be comparatively low, consistent with previous reports from Korea. However our trials, performed with a variety of diagnostic tools, were considered to be useful for the precise diagnosis of congenital toxoplasmosis.

Citations

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Original Articles

Protective efficacy of vaccination with Neospora caninum multiple recombinant antigens against experimental Neospora caninum infection: Jung-Hwa Cho, Woo-Suk Chung, Kyoung-Ju Song, Byoung-Kuk Na, Seung-Won Kang, Chul-Yong Song, Tong-Soo Kim; Korean J Parasitol 2005;43(1):19-25.
Published online March 20, 2005; DOI: https://doi.org/10.3347/kjp.2005.43.1.19

Abstract
PDF

Protective efficacy of vaccination with Neospora caninum multiple recombinant antigens against N. caninum infection was evaluated in vitro and in vivo. Two major immunodominant surface antigens (NcSAG1 and NcSRS2) and two dense granule proteins (NcDG1 and NcDG2) of N. caninum tachyzoites were expressed in E. coli, respectively. An in vitro neutralization assay using polyclonal antisera raised against each recombinant antigen showed inhibitory effects on the invasion of N. caninum tachyzoites into host cells. Separate groups of gerbils were immunized with the purified recombinant proteins singly or in combinations and animals were then challenged with N.caninum. Following these experimental challenges, the protective efficacy of each vaccination was determined by assessing animal survival rate. All experimental groups showed protective effects of different degrees against experimental infection. The highest protection efficacy was observed for combined vaccination with NcSRS2 and NcDG1. Our results indicate that combined vaccination with the N. caninum recombinant antigens, NcSRS2 and NcDG1, induces the highest protective effect against N. caninum infection in vitro and in vivo.

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Decreasing effect of an anti-Nfa1 polyclonal antibody on the in vitro cytotoxicity of pathogenic Naegleria fowleri: Seok-Ryoul Jeong, Su-Yeon Kang, Sang-Chul Lee, Kyoung-Ju Song, Kyung-il Im, Ho-Joon Shin; Korean J Parasitol 2004;42(1):35-40.
Published online March 20, 2004; DOI: https://doi.org/10.3347/kjp.2004.42.1.35

Abstract
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The nfa1 gene was cloned from a cDNA library of pathogenic Naegleria fowleri by immunoscreening; it consisted of 360 bp and produced a 13.1 kDa recombinant protein (rNfa1) that showed the pseudopodia-specific localization by immunocytochemistry in the previous study. Based on the idea that the pseudopodia-specific Nfa1 protein mentioned above seems to be involved in the pathogenicity of N. fowleri, we observed the effect of an anti-Nfa1 antibody on the proliferation of N. fowleri trophozoites and the cytotoxicity of N. fowleri trophozoites on the target cells. The proliferation of N. fowleri trophozoites was inhibited after being treated with an anti-Nfa1 polyclonal antibody in a dose-dependent manner for 48 hrs. By a light microscope, CHO cells co-cultured with N. fowleri trophozoites (group I) for 48 hrs showed severe morphological destruction. On the contrary, CHO cells co-cultured with N. fowleri trophozoites and anti-Nfa1 polyclonal antibody (1:100 dilution) (group II) showed less destruction. In the LDH release assay results, group I showed 50.6% cytotoxicity, and group II showed 39.3%. Consequently, addition of an anti-Nfa1 polyclonal antibody produced a decreasing effect of in vitro cytotoxicity of N. fowleri in a dosedependent manner.

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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

Abstract
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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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Molecular cloning and characterization of peroxiredoxin from Toxoplasma gondii: Eui-Sun Son, Kyoung-Ju Song, Jong-Chul Shin, Ho-Woo Nam; Korean J Parasitol 2001;39(2):133-141.
Published online June 30, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.2.133

Abstract
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A cDNA of 1.1 kb comprising the gene encoding the peroxiredoxin of Toxoplasma gondii (TgPrx) has been cloned. The open reading frame of 591 bp was translated into a protein of 196 amino acids with a molecular mass of 25 kDa. Conserved 2 cysteine domains of Phe-Val-Cys-Pro and Glu-Val-Cys-Pro indicated TgPrx belonged to 2-Cys Prx families. TgPrx showed the highest homology with that of Arabidopsis thaliana by 53.9% followed by Entamoeba histolytica with 39.5% by the amino acid sequence alignment. Polyclonal antibody against recombinant TgPrx detected 25 kDa band in T. gondii without binding to host cell proteins. TgPrx was located in the cytoplasm of T. gondii extracellularly or intracellularly by immunofluorescence assay. The expression of TgPrx was increased as early as 30 min after the treatment with artemisinin in the intracellular stage, while no changes in those of host Prx I and TgSOD. This result implies that TgPrx may function as an antioxidant protecting the cell from the attack of reactive oxygen intermediates. It is also suggested that TgPrx is a possible target of chemotherapy.

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Experimental Parasitology.2009; 122(1): 41. CrossRef
Dual Targeting of Antioxidant and Metabolic Enzymes to the Mitochondrion and the Apicoplast of Toxoplasma gondii
Paco Pino, Bernardo Javier Foth, Lai-Yu Kwok, Lilach Sheiner, Rebecca Schepers, Thierry Soldati, Dominique Soldati-Favre, Daniel Eliot Goldberg
PLoS Pathogens.2007; 3(8): e115. CrossRef
Plasmodium falciparum: Discovery of peroxidase active organelles
Michael T. McIntosh, David A. Elliott, Keith A. Joiner
Experimental Parasitology.2005; 111(2): 133. CrossRef
Host persistence: exploitation of anti-inflammatory pathways by Toxoplasma GONDII
Julio Aliberti
Nature Reviews Immunology.2005; 5(2): 162. CrossRef
The Opportunistic Pathogen Toxoplasma gondii Deploys a Diverse Legion of Invasion and Survival Proteins
Xing W. Zhou, Björn F.C. Kafsack, Robert N. Cole, Phil Beckett, Rong F. Shen, Vern B. Carruthers
Journal of Biological Chemistry.2005; 280(40): 34233. CrossRef
The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury
Lai Yu Kwok, Dirk Schlüter, Christine Clayton, Dominique Soldati
Molecular Microbiology.2004; 51(1): 47. CrossRef