Parasites, Hosts and Diseases

"Eui-Sun Son"

Original Articles

Determination of antigenic domain in GST fused major surface protein (Nc-p43) of Neospora caninum: Eui-Sun Son, Hye-Jin Ahn, Jae-Hoon Kim, Dae-Yong Kim, Ho-Woo Nam; Korean J Parasitol 2001;39(3):241-246.
Published online September 30, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.3.241

Abstract
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The antigenic domain of the major surface protein (Nc-p43) of Neospora caninum was examined by polymerase chain reaction of its gene fragments and recombinant expression as GST fusion proteins. The fragments of Nc-p43 were as follow: a total open reading frame (OFR), T; OFR without signal sequence and C-terminal hydrophobic sequence, S; N-terminal 2/3 parts of S, A; C-terminal 2/3 parts, P; N-terminal 1/3 part, X; middle 1/3 part, Y; and C-terminal 1/3 part, Z, respectively. The DNA fragments were cloned into pGEX-4T vector. Recombinant plasmids transformed into Escherichia coli of BL21 pLysS (DE3) strain were induced to express GST or GST fused fragments of Nc-p43 such as 69 kDa protein for T, 66 kDa for S, 52 kDa for A, 53 kDa for P, and 40 kDa proteins for X, Y, and Z, respectively in SDS-PAGE. The Nc-p43 fragments of T, S, and P reacted with a bovine serum of neosporosis while those of A, X, Y, and Z together with GST did not in the western blot. These findings suggest that the antigenic domain of Nc-p43 of N. caninum may be localized in the C-terminal 2/3 parts. Together with A19 clone in SAG1 of Toxoplasma gondii (Nam et al., 1996), the P fragment of Nc-p43 could be used as efficient antigens to diagnose and differentiate those infections with both species.

Citations

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Molecular characterization of Neospora caninum major antigens NcSAG1 and NcSRS2
Soledad Echeverría, Federico Carrión, Martín Soñora, Andrés Cabrera, Carlos Robello
Royal Society Open Science.2025;[Epub] CrossRef
Expression ofNeospora caninumNcSRS2 surface protein inPichia pastorisand its application for serodiagnosis ofNeosporainfection
Amanda Fernandes Pinheiro, Sibele Borsuk, Maria Elisabeth Aires Berne, Luciano da Silva Pinto, Renato Andreotti, Talita Roos, Barbara Couto Rollof, Fábio Pereira Leivas Leite
Pathogens and Global Health.2013; 107(3): 116. CrossRef
Induction of Interferon-Gamma (IFN-γ) and T Helper 1 (Th1) Immune Response by Bitter Gourd Extract
Kazunori IKE, Yuko UCHIDA, Tomohiko NAKAMURA, Soichi IMAI
Journal of Veterinary Medical Science.2005; 67(5): 521. CrossRef
ELISA detection of IgG antibody against a recombinant major surface antigen (Nc-p43) fragment of Neospora caninum in bovine sera
Hye-Jin Ahn, Sera Kim, Dae-Yong Kim, Ho-Woo Nam
The Korean Journal of Parasitology.2003; 41(3): 175. CrossRef

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Western blot diagnosis of vivax malaria with multiple stage-specific antigens of the parasite: Eui-Sun Son, Tong Soo Kim, Ho-Woo Nam; Korean J Parasitol 2001;39(2):171-176.
Published online June 30, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.2.171

Abstract
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Western blot analysis was performed to diagnose vivax malaria using stage-specific recombinant antigens. Genomic DNA from the whole blood of a malaria patient was used as templates to amplify the coding regions for the antigenic domains of circumsporozoite protein (CSP-1), merozoite surface protein (MSP-1), apical merozoite antigen (AMA-1), serine repeat antigen (SERA), and exported antigen (EXP-1) of Plasmodium vivax. Each amplified DNA fragment was inserted into a pGEX-4T plasmid to induce the expression of GST fusion protein in Escherichia coli by IPTG. The bacterial cell extracts were separated on 10% SDS-PAGE followed by western blot analysis with patient sera which was confirmed by blood smear examination. When applied with patient sera, 147 (91.9%) out of 160 vivax malaria, 12 (92.3%) out of 13 falciparum malaria, and all 9 vivax/falciparum mixed malaria reacted with at least one antigen, while no reactions occurred with 20 normal uninfected sera. In the case of vivax malaria, CSP-1 reacted with 128 (80.0%) sera, MSP-1 with 102 (63.8%), AMA-1 with 128 (80.0%), SERA with 115 (71.9%), and EXP-1 with 89 (55.6%), respectively. We obtained higher detection rates when using 5 antigens (91.9%) rather than using each antigen solely (55.6-80%), a combination of 2 (76.3-87.5%), 3 (85.6-90.6%), or 4 antigens (89.4-91.3%). This method can be applied to serological diagnosis, mass screening in endemic regions, or safety test in transfusion of prevalent vivax malaria.

Citations

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A Dual, Systematic Approach to Malaria Diagnostic Biomarker Discovery
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The American Journal of Tropical Medicine and Hygiene.2013; 88(5): 835. CrossRef
Identification of Plasmodium vivax Proteins with Potential Role in Invasion Using Sequence Redundancy Reduction and Profile Hidden Markov Models
Daniel Restrepo-Montoya, David Becerra, Juan G. Carvajal-Patiño, Alvaro Mongui, Luis F. Niño, Manuel E. Patarroyo, Manuel A. Patarroyo, Leonardo Mariño-Ramírez
PLoS ONE.2011; 6(10): e25189. CrossRef
ELISA detection of vivax malaria with recombinant multiple stage-specific antigens and its application to survey of residents in endemic areas
Sera Kim, Hye-Jin Ahn, Tong-Soo Kim, Ho-Woo Nam
The Korean Journal of Parasitology.2003; 41(4): 203. CrossRef

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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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Detection and characterization of excretory/secretory proteins from Toxoplasma gondii by monoclonal antibodies: Eui-Sun Son, Ho-Woo Nam; Korean J Parasitol 2001;39(1):49-56.
Published online March 31, 2001; DOI: https://doi.org/10.3347/kjp.2001.39.1.49

Abstract
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Excretory/secretory proteins (ESP) from Toxoplasma gondii were analyzed to define the function in the penetration process into host cells. Whole ESP obtained at 37℃ were composed of 15 bands with molecular mass of 110, 97, 86, 80, 70, 60, 54, 42, 40, 36, 30, 28, 26, 22, and 19 kDa. Five ESP of 86, 80, 42, 36, and 28 kDa were reacted with monoclonal antibodies (mAb), named as Tg386 (microneme), Tg485 (surface membrane), Tg786 (rhoptry), Tg378, and Tg556 (both dense granules), respectively. The ESP was released by a temperature-dependent/-independent manner and all at once whenever ready to pour out except Tg786. Each ESP was not exhausted within the parasite but the amount was limited. Tg786 was released continuously with increment, whereas Tg378 and Tg556 were ceased to release after 3 and 4 hr. Dense granular Tg378 and Tg556 were released spontaneously and constitutively before the entry into host cells also. The entry of T. gondii was inhibited by all the mAbs differentially. And the parasite deprived of ESP was inhibited to enter exponentially up to 90.1%. It is suggested that ESP play an essential function to provide appropriate environment for the entry of the parasite into host cells.

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