Parasites, Hosts and Diseases

"Yeon-Chul Hong"

Brief Communication

Prevalence of Trichomoniasis by PCR in Women Attending Health Screening in Korea: Seung-Ryong Kim, Jung-Hyun Kim, Na-Yeong Gu, Yong-Suk Kim, Yeon-Chul Hong, Jae-Sook Ryu; Korean J Parasitol 2016;54(2):187-190.
Published online April 30, 2016; DOI: https://doi.org/10.3347/kjp.2016.54.2.187

Abstract
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Trichomoniasis is the most common curable sexually-transmitted infection (STI) worldwide. There are few reports on the prevalence of Trichomonas vaginalis in Korea. The purpose of this study was to examine the prevalence of trichomoniasis by PCR in Guri city, Korea. All adult women who visited Hanyang University Guri Hospital for health screening within the National Health Care Service were invited to participate in the study, and 424 women were enrolled between March and June 2011. PCR was used to detect Trichomonas vaginalis using primers based on a repetitive sequence cloned from T. vaginalis (TV-E650). Fourteen women (3.3%) were found to have T. vaginalis. All were over 50, and they were significantly older on average than the 410 Trichomonas-negative women (mean ages 63.4 vs 55.3 years). It seems that T. vaginalis infection is not rare in women receiving health screening, especially among those over 50.

Citations

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Construction a novel detection method for Trichomonas vaginalis based on recombinant enzyme polymerase amplification targeting the Actin gene
Fakun Li, Yangyang Deng, Wanxin Sheng, Xihui Gao, Weijuan Wang, Zhili Chu, Xuefang Mei, Zhenke Yang, Xiaowei Tian, Shuai Wang, Zhenchao Zhang
Journal of Eukaryotic Microbiology.2023;[Epub] CrossRef
Molecular characterization of Trichomonas infections in women of Ilam City, southwestern Iran
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Parasitology Research.2022; 121(6): 1631. CrossRef
Status of common parasitic diseases in Korea in 2019
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Journal of the Korean Medical Association.2019; 62(8): 437. CrossRef

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Original Articles

Construction of EST Database for Comparative Gene Studies of Acanthamoeba: Eun-Kyung Moon, Joung-Ok Kim, Ying-Hua Xuan, Young-Sun Yun, Se Won Kang, Yong Seok Lee, Tae-In Ahn, Yeon-Chul Hong, Dong-Il Chung, Hyun-Hee Kong; Korean J Parasitol 2009;47(2):103-107.
Published online May 26, 2009; DOI: https://doi.org/10.3347/kjp.2009.47.2.103

Abstract
PDF

The genus Acanthamoeba can cause severe infections such as granulomatous amebic encephalitis and amebic keratitis in humans. However, little genomic information of Acanthamoeba has been reported. Here, we constructed Acanthamoeba expressed sequence tags (EST) database (Acanthamoeba EST DB) derived from our 4 kinds of Acanthamoeba cDNA library. The Acanthamoeba EST DB contains 3,897 EST generated from amebae under various conditions of long term in vitro culture, mouse brain passage, or encystation, and downloaded data of Acanthamoeba from National Center for Biotechnology Information (NCBI) and Taxonomically Broad EST Database (TBestDB). The almost reported cDNA/genomic sequences of Acanthamoeba provide stand alone BLAST system with nucleotide (BLAST NT) and amino acid (BLAST AA) sequence database. In BLAST results, each gene links for the significant information including sequence data, gene orthology annotations, relevant references, and a BlastX result. This is the first attempt for construction of Acanthamoeba database with genes expressed in diverse conditions. These data were integrated into a database (http://www.amoeba.or.kr).

Citations

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Frontiers in Microbiology.2023;[Epub] CrossRef
Autophagy protein 12 plays an essential role in Acanthamoeba encystation
So-Hee Kim, Eun-Kyung Moon, Yeonchul Hong, Dong-Il Chung, Hyun-Hee Kong
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Caspase-like proteins: Acanthamoeba castellanii metacaspase and Dictyostelium discoideum paracaspase, what are their functions?
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Helminth parasites of fish and shellfish from the Santa Gilla Lagoon in southern Sardinia, Italy
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Experimental Parasitology.2014; 143: 69. CrossRef
Protein kinase C signaling molecules regulate encystation of Acanthamoeba
Eun-Kyung Moon, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong
Experimental Parasitology.2012; 132(4): 524. CrossRef
Microarray Analysis of Differentially Expressed Genes between Cysts and Trophozoites ofAcanthamoeba castellanii
Eun-Kyung Moon, Ying-Hua Xuan, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong
The Korean Journal of Parasitology.2011; 49(4): 341. CrossRef
Drug target identification, validation, characterisation and exploitation for treatment of Acanthamoeba (species) infections
Craig W. Roberts, Fiona L. Henriquez
Experimental Parasitology.2010; 126(1): 91. CrossRef
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Yong-Seok Lee, Moon-Ki Baek, Yong-Hun Jo, Se-Won Kang, Jae-Bong Lee, Yeon-Soo Han, Hee-Jae Cha, Hak-Sun Yu, Mee-Sun Ock
Journal of Life Science.2010; 20(3): 411. CrossRef

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Keratitis by Acanthamoeba triangularis: Report of Cases and Characterization of Isolates: Ying-Hua Xuan, Byung-Suk Chung, Yeon-Chul Hong, Hyun-Hee Kong, Tae-Won Hahn, Dong-Il Chung; Korean J Parasitol 2008;46(3):157-164.
Published online September 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.3.157

Abstract
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Three Acanthamoeba isolates (KA/E9, KA/E17, and KA/E23) from patients with keratitis were identified as Acanthamoeba triangularis by analysis of their molecular characteristics, a species not previously recognized to be a corneal pathogen. Epidemiologic significance of A. triangularis as a keratopathogen in Korea has been discussed. Morphologic features of Acanthamoeba cysts were examined under a microscope with differential interference contrast (DIC) optics. Mitochondrial DNA (mtDNA) of the ocular isolates KA/E9, KA/E17, and KA/E23 were digested with restriction enzymes, and the restriction patterns were compared with those of reference strains. Complete nuclear 18S and mitochondrial (mt) 16S rDNA sequences were subjected to phylogenetic analysis and species identification. mtDNA RFLP of 3 isolates showed very similar patterns to those of SH621, the type strain of A. triangularis. 16S and 18S rDNA sequence analysis confirmed 3 isolates to be A. triangularis. 18S rDNA sequence differences of the isolates were 1.3% to 1.6% and those of 16S rDNA, 0.4% to 0.9% from A. triangularis SH621. To the best of our knowledge, this is the first report, confirmed by 18S and 16S rDNA sequence analysis, of keratitis caused by A. triangularis of which the type strain was isolated from human feces. Six isolates of A. triangularis had been reported from contaminated contact lens cases in south eastern Korea.

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The First Case of Cutaneous Acanthamoebiasis Caused by Acanthamoeba triangularis in Korea
Mi Soo Choi, Na Hye Myong, Min Seo, Sukbin Jang, Dae Kwan Yun, Kyujin Yeom, Dong-Il Chung, Byung Cheol Park, Yeonchul Hong, Myung Hwa Kim
Annals of Dermatology.2023; 35(Suppl 2): S275. CrossRef
Detection of Acanthamoeba spp. using carboxylesterase antibody and its usage for diagnosing Acanthamoeba-keratitis
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Brief Communication

Differentially expressed genes of Acanthamoeba castellanii during encystation: Eun-Kyung Moon, Dong-Il Chung, Yeon-Chul Hong, Hyun-Hee Kong; Korean J Parasitol 2007;45(4):283-285.
Published online December 20, 2007; DOI: https://doi.org/10.3347/kjp.2007.45.4.283

Abstract
PDF

To examine the expressed gene profile during encystation of Acanthamoeba castellanii Castellani, we used differentially expressed gene (DGE) screening by RT-PCR with 20 sets of random primers. From this analysis, we found that approximately 16 genes showed upregulation during encystation. We chose 6 genes, which had relatively higher expression levels, for further investigation. Based on homology search in database, DEG2 showed 55% of similarity with xylose isomerase, DEG9 showed 37% of similarity with Na P-type ATPase, and DEG14 showed 77% of similarity with subtilisin-like serine proteinase. DEG3 and DEG26 were identified as hypothetical proteins and DEG25 exhibited no significant similarity to any known protein. Encystation of Acanthamoeba has been suggested to be a process to resist adverse environmental or nutritional conditions. Further characterization studies of these genes may provide us with more information on the encystation mechanism of Acanthamoeba.

Citations

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Encystment and Excystment Processes in Acanthamoeba castellanii: An Emphasis on Cellulose Involvement
Mathew Choaji, Ascel Samba-Louaka, Zineb Fechtali-Moute, Willy Aucher, Sébastien Pomel
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Oxidase enzyme genes are differentially expressed during Acanthamoeba castellanii encystment
Christian Q. Scheckhuber, Rebeca Damián Ferrara, Jesús Gómez-Montalvo, Sutherland K. Maciver, Alvaro de Obeso Fernández del Valle
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Kuang-Yi Shih, Yao-Tsung Chang, Yu-Jen Wang, Jian-Ming Huang
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Bader Saleem Alawfi, Naveed Ahmed Khan, David Lloyd, Ruqaiyyah Siddiqui
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Yuehua Wang, Linzhe Jiang, Yitong Zhao, Xiaohong Ju, Le Wang, Liang Jin, Ryan D. Fine, Mingguang Li
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mRNA Sequencing Reveals Upregulation of Glutathione S-Transferase Genes during Acanthamoeba Encystation
Alvaro de Obeso Fernández del Valle, Christian Quintus Scheckhuber, David Armando Chavaro-Pérez, Erandi Ortega-Barragán, Sutherland K. Maciver
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Zineb Fechtali-Moute, Philippe M. Loiseau, Sébastien Pomel
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Down-Regulation of Cellulose Synthase Inhibits the Formation of Endocysts in Acanthamoeba
Eun-Kyung Moon, Yeonchul Hong, Dong-Il Chung, Youn-Kyoung Goo, Hyun-Hee Kong
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Protein kinase C signaling molecules regulate encystation of Acanthamoeba
Eun-Kyung Moon, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong
Experimental Parasitology.2012; 132(4): 524. CrossRef
Cellular, Biochemical, and Molecular Changes during Encystment of Free-Living Amoebae
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Microarray Analysis of Differentially Expressed Genes between Cysts and Trophozoites ofAcanthamoeba castellanii
Eun-Kyung Moon, Ying-Hua Xuan, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong
The Korean Journal of Parasitology.2011; 49(4): 341. CrossRef
Major Role for Cysteine Proteases during the Early Phase of Acanthamoeba castellanii Encystment
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Characterization of a Serine Proteinase Mediating Encystation of Acanthamoeba
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Original Articles

Natural occurrence of Mycobacterium as an endosymbiont of Acanthamoeba isolated from a contact lens storage case: Hak Sun Yu, Hae Jin Jeong, Yeon-Chul Hong, Seong-Yong Seol, Dong-Il Chung, Hyun-Hee Kong; Korean J Parasitol 2007;45(1):11-18.
Published online March 20, 2007; DOI: https://doi.org/10.3347/kjp.2007.45.1.11

Abstract
PDF

Recent in vitro studies have revealed that a certain Mycobacterium can survive and multiply within free-living amoebae. It is believed that protozoans function as host cells for the intracellular replication and evasion of Mycobacterium spp. under harmful conditions. In this study, we describe the isolation and characterization of a bacterium naturally observed within an amoeba isolate acquired from a contact lens storage case. The bacterium multiplied within Acanthamoeba, but exerted no cytopathic effects on the amoeba during a 6-year amoebic culture. Trasnmission electron microscopy showed that the bacteria were randomly distributed within the cytoplasm of trophozoites and cysts of Acanthamoeba. On the basis of the results of 18S rRNA gene analysis, the amoeba was identified as A. lugdunensis. A 16S rRNA gene analysis placed this bacterium within the genus Mycobacterium. The bacterium evidenced positive reactivity for acid-fast and fluorescent acid-fast stains. The bacterium was capable of growth on the Middlebrook 7H11-Mycobacterium-specific agar. The identification and characterization of bacterial endosymbionts of free-living protozoa bears significant implications for our understanding of the ecology and the identification of other atypical mycobacterial pathogens.

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Molecular and biochemical characterization of a novel actin bundling protein in Acanthamoeba: Joanna It-itan Alafag, Eun-Kyung Moon, Yeon-Chul Hong, Dong-Il Chung, Hyun-Hee Kong; Korean J Parasitol 2006;44(4):331-341.
Published online December 20, 2006; DOI: https://doi.org/10.3347/kjp.2006.44.4.331

Abstract
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Actin binding proteins play key roles in cell structure and movement particularly as regulators of the assembly, stability and localization of actin filaments in the cytoplasm. In the present study, a cDNA clone encoding an actin bundling protein named as AhABP was isolated from Acanthamoeba healyi, a causative agent of granulomatous amebic encephalitis. This clone exhibited high similarity with genes of Physarum polycephalum and Dictyostelium discoideum, which encode actin bundling proteins. Domain search analysis revealed the presence of essential conserved regions, i.e., an active actin binding site and 2 putative calcium binding EF-hands. Transfected amoeba cells demonstrated that AhABP is primarily localized in phagocytic cups, peripheral edges, pseudopods, and in cortical cytoplasm where actins are most abundant. Moreover, AhABP after the deletion of essential regions formed ellipsoidal inclusions within transfected cells. High-speed co-sedimentation assays revealed that AhABP directly interacted with actin in the presence of up to 10 ?M of calcium. Under the electron microscope, thick parallel bundles were formed by full length AhABP, in contrast to the thin actin bundles formed by constructs with deletion sites. In the light of these results, we conclude that AhABP is a novel actin bundling protein that is importantly associated with actin filaments in the cytoplasm.

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Abdul Mannan Baig, Junaid Iqbal, Naveed Ahmed Khan
Antimicrobial Agents and Chemotherapy.2013; 57(8): 3561. CrossRef

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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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Suman Dahal, Pratibha Gour, Saurabh Raghuvanshi, Yugal Kishore Prasad, Dipshikha Saikia, Sudeep Ghatani
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Kurt C. Curtis, Kerstin Fischer, Young-Jun Choi, Makedonka Mitreva, Gary J. Weil, Peter U. Fischer
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Conor R. Caffrey, Louise Goupil, Karina M. Rebello, John P. Dalton, David Smith, Aaron R. Jex
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International Journal of Infectious Diseases.2008; 12(6): e49. CrossRef

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Evaluation of taxonomic validity of four species of Acanthamoeba: A. divionensis, A. paradivionensis, A. mauritaniensis, and A. rhysodes, inferred from molecular analyses: Hua Liu, Eun-Kyung Moon, Hak-Sun Yu, Hae-Jin Jeong, Yeon-Chul Hong, Hyun-Hee Kong, Dong-Il Chung; Korean J Parasitol 2005;43(1):7-13.
Published online March 20, 2005; DOI: https://doi.org/10.3347/kjp.2005.43.1.7

Abstract
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The taxonomy of Acanthamoeba spp., an amphizoic amoeba which causes granulomatous amoebic encephalitis and chronic amoebic keratitis, has been revised many times. The taxonomic validity of some species has yet to be assessed. In this paper, we analyzed the morphological characteristics, nuclear 18s rDNA and mitochondrial 16s rDNA sequences and the Mt DNA RFLP of the type strains of four Acanthamoeba species, which had been previously designated as A. divionensis, A. parasidionensis, A. mauritaniensis, and A. rhysodes. The four isolates revealed characteristic group II morphology. They exhibited 18S rDNA sequence differences of 0.2-1.1% with each other, but more than 2% difference from the other compared reference strains. Four isolates formed a different clade from that of A. castellanii Castellani and the other strains in morphological group II on the phylogenetic tree. In light of these results, A. paradivionensis, A. divionensis, and A. mauritaniensis should be regarded as synonyms for A. rhysodes.

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The Korean Journal of Parasitology.2008; 46(3): 157. CrossRef
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Hatice Ertabaklar, Meral Türk, Volkan Dayanir, Sema Ertuğ, Julia Walochnik
Parasitology Research.2007; 100(2): 241. CrossRef

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Isolation and characterization of a cDNA encoding a mammalian cathepsin L-like cysteine proteinase from Acanthamoeba healyi: Yeon-Chul Hong, Mi-Yul Hwang, Ho-Cheol Yun, Hak-Sun Yu, Hyun-Hee Kong, Tai-Soon Yong, Dong-Il Chung; Korean J Parasitol 2002;40(1):17-24.
Published online March 31, 2002; DOI: https://doi.org/10.3347/kjp.2002.40.1.17

Abstract
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We have cloned a cDNA encoding a cysteine proteinase of the Acanthamoeba healyi OC-3A strain isolated from the brain of a granulomatous amoebic encephalitis patient. A DNA probe for an A. healyi cDNA library screening was amplified by PCR using degenerate oligonucleotide primers designed on the basis of conserved amino acids franking the active sites of cysteine and asparagine residues that are conserved in the eukaryotic cysteine proteinases. Cysteine proteinase gene of A. healyi (AhCP1) was composed of 330 amino acids with signal sequence, a proposed pro-domain and a predicted active site made up of the catalytic residues, Cys²⁵, His¹⁵⁹, and Asn¹⁷⁵. Deduced amino acid sequence analysis indicates that AhCP1 belong to ERFNIN subfamily of C1 peptidases. By Northern blot analysis, no direct correlation was observed between AhCP1 mRNA expression and virulence of Acanthamoeba, but the gene was expressed at higher level in amoebae isolated from soil than amoeba from clinical samples. These findings raise the possibility that Ahcp1 protein may play a role in protein metabolism and digestion of phagocytosed bacteria or host tissue debris rather than in invasion of amoebae into host tissue.

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Acanthamoeba culbertsoni Elicits Soluble Factors That Exert Anti-Microglial Cell Activity
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Characterization of a Serine Proteinase Mediating Encystation of Acanthamoeba
Eun-Kyung Moon, Dong-Il Chung, Yeon-Chul Hong, Hyun-Hee Kong
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