Parasites, Hosts and Diseases

"SAG1"

Original Articles

Evaluation of Recombinant SAG1, SAG2, and SAG3 Antigens for Serodiagnosis of Toxoplasmosis: Khadijeh Khanaliha, Mohammad Hossein Motazedian, Bahram Kazemi, Bahador Shahriari, Mojgan Bandehpour, Zarin Sharifniya; Korean J Parasitol 2014;52(2):137-142.
Published online April 18, 2014; DOI: https://doi.org/10.3347/kjp.2014.52.2.137

Abstract
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Serologic tests are widely accepted for diagnosing Toxoplasma gondii but purification and standardization of antigen needs to be improved. Recently, surface tachyzoite and bradyzoite antigens have become more attractive for this purpose. In this study, diagnostic usefulness of 3 recombinant antigens (SAG1, SAG2, and SAG3) were evaluated, and their efficacy was compared with the available commercial ELISA. The recombinant plasmids were transformed to JM109 strain of Escherichia coli, and the recombinants were expressed and purified. Recombinant SAG1, SAG2, and SAG3 antigens were evaluated using different groups of sera in an ELISA system, and the results were compared to those of a commercial IgG and IgM ELISA kit. The sensitivity and specificity of recombinant surface antigens for detection of anti-Toxoplasma IgG in comparison with commercially available ELISA were as follows: SAG1 (93.6% and 92.9%), SAG2 (100.0% and 89.4%), and SAG3 (95.4% and 91.2%), respectively. A high degree of agreement (96.9%) was observed between recombinant SAG2 and commercial ELISA in terms of detecting IgG anti-Toxoplasma antibodies. P22 had the best performance in detecting anti-Toxoplasma IgM in comparison with the other 2 recombinant antigens. Recombinant SAG1, SAG2, and SAG3 could all be used for diagnosis of IgG-specific antibodies against T. gondii.

Citations

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IgM Antibody Detection as a Diagnostic Marker for Acute Toxoplasmosis: Current Status of Studies and Main Limitations
Karolina Sołowińska, Lucyna Holec-Gąsior
Antibodies.2025; 14(2): 44. CrossRef
Analysis of the Correlation Between Toxoplasma gondii Seropositivity and Alzheimer’s Disease
Jianjun Wang, Ping Lin, Dan Li, Biyu Yang, Jiaqi Wang, Meng Feng, Xunjia Cheng
Pathogens.2024; 13(11): 1021. CrossRef
Seroprevalence and Epidemiology of Toxoplasma gondii in Animals in the Qinghai-Tibetan Plateau Area, China
Guojing Li, Wangli Zheng, Jinfang Yang, Tongsheng Qi, Yongcai He, Wangkai Chen, Hejia Ma, Yali Sun, Ying Li, Ming Kang, Jixu Li
Pathogens.2021; 10(4): 432. CrossRef
Detection of Toxoplasma gondii Infections using Virus-Like Particles Displaying T. gondii ROP4 Antigen
Min-Ju Kim, Jie Mao, Hae-Ji Kang, Ki-Back Chu, Fu-Shi Quan
The Korean Journal of Parasitology.2021; 59(6): 565. CrossRef
Prevalence of Toxoplasma gondii parasite in captive Mexican jaguars determined by recombinant surface antigens (SAG1) and dense granular antigens (GRA1 and GRA7) in ELISA-based serodiagnosis
Alejandro Reynoso-Palomar, Dulce Moreno-Gálvez, Abel Villa-Mancera
Experimental Parasitology.2020; 208: 107791. CrossRef
Evaluation of a PCR assay for diagnosis of toxoplasmosis in serum and peripheral blood mononuclear cell among HIV/AIDS patients
Farah Bokharaei-Salim, Abdoulreza Esteghamati, Khadijeh Khanaliha, Saeed Kalantari, Shirin Sayyahfar, Tahereh Donyavi, Saba Garshasbi, Qasem Asgari, Borna Salemi
Journal of Parasitic Diseases.2020; 44(1): 159. CrossRef
Toxoplasma gondii seropositivity and serointensity and cognitive function in adults
Shawn D. Gale, Lance D. Erickson, Evan L. Thacker, Elizabeth L. Mitchell, Bruce L. Brown, Dawson W. Hedges, Mathieu Nacher
PLOS Neglected Tropical Diseases.2020; 14(10): e0008733. CrossRef
Human toxoplasmosis in Mozambique: gaps in knowledge and research opportunities
Leonardo Manuel, Gabriela Santos-Gomes, Emilia V. Noormahomed
Parasites & Vectors.2020;[Epub] CrossRef
The soluble fraction of Neospora caninum treated with PI-PLC is dominated by NcSRS29B and NcSRS29C
Marcos Alexandre Bezerra, Luiz Miguel Pereira, Luciana Baroni, Ana Patrícia Yatsuda
Experimental Parasitology.2019; 204: 107731. CrossRef
Research Progress of Antigens Related to the Process of Toxoplasma gondii Invading Host Cell
晓敬孙
Open Journal of Natural Science.2019; 07(06): 585. CrossRef
Toxoplasma gondii-positive human sera recognise intracellular tachyzoites and bradyzoites with diverse patterns of immunoreactivity
Marijo S. Roiko, Kaice LaFavers, Diane Leland, Gustavo Arrizabalaga
International Journal for Parasitology.2018; 48(3-4): 225. CrossRef
Development of an immunochromatographic test based on monoclonal antibodies against surface antigen 3 (TgSAG3) for rapid detection of Toxoplasma gondii
Jiaqing Luo, Hongchao Sun, Xianfeng Zhao, Suhua Wang, Xunhui Zhuo, Yi Yang, Xueqiu Chen, Chaoqun Yao, Aifang Du
Veterinary Parasitology.2018; 252: 52. CrossRef
Antigens to Detect the Acute Phase of Toxoplasmosis in Pregnant Women: Standardized Comparison
Juan Gabriel Costa, María Julia Vilariño
Biomarkers in Medicine.2018; 12(5): 517. CrossRef
P35 and P22 Toxoplasma gondii antigens abbreviate regions to diagnose acquired toxoplasmosis during pregnancy: toward single-sample assays
Juan G. Costa, Leandro E. Peretti, Valeria S. García, Luz Peverengo, Verónica D.G. González, Luis M. Gugliotta, Maria L. Dalla Fontana, Claudia M. Lagier, Iván S. Marcipar
Clinical Chemistry and Laboratory Medicine (CCLM).2017;[Epub] CrossRef
Cloning and Sequencing of Truncated Toxoplasma gondii Subtilisin-Like 1 Antigen
Ahmad Rouhizadeh, Ata A Ghadiri, Mohammad Razi Jalali, Masoud Ghorbanpour, Mohammad Hossein Razi Jalali
Zahedan Journal of Research in Medical Sciences.2016;[Epub] CrossRef
Evaluation of Recombinant SRS3 Antigen for Diagnosis of Toxoplasmosis by Enzyme-Linked Immunosorbent Assay
Seyedeh Mahya Marashiyan, Fatemeh Moradian, Geita Saadatnia, Majid Golkar
Archives of Clinical Infectious Diseases.2016;[Epub] CrossRef
Cloning and Expression of Major Surface Antigen 1 Gene of Toxoplasma gondii RH Strain Using the Expression Vector pVAX1 in Chinese Hamster Ovary Cells
Rahman Abdizadeh, Sharif Maraghi, Ata A. Ghadiri, Mehdi Tavalla, Saeedeh Shojaee
Jundishapur Journal of Microbiology.2015;[Epub] CrossRef

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Crossref

A Rapid Diagnostic Test for Toxoplasmosis using Recombinant Antigenic N-terminal Half of SAG1 Linked with Intrinsically Unstructured Domain of GRA2 Protein: Kyoung Ju Song, Zhaoshou Yang, Chom-Kyu Chong, Jin-Soo Kim, Kyung Chan Lee, Tong-Soo Kim, Ho-Woo Nam; Korean J Parasitol 2013;51(5):503-510.
Published online October 31, 2013; DOI: https://doi.org/10.3347/kjp.2013.51.5.503

Abstract
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Toxoplasma gondii is an apicomplexan parasite with a broad host range of most warm-blooded mammals including humans, of which one-thirds of the human population has been infected worldwide which can cause congenital defects, abortion, and neonatal complications. Here, we developed a rapid diagnostic test (RDT) for T. gondii infection. Antigenic N-terminal half of the major surface antigen (SAG1) was linked with intrinsically unstructured domain (IUD) of dense granule protein 2 (GRA2). The recombinant GST-GRA2-SAG1A protein was successfully expressed and purified as 51 kDa of molecular weight. Furthermore, antigenicity and solubility of the rGST-GRA2-SAG1A protein were significantly increased. The overall specificity and sensitivity of GST-GRA2-SAG1A loaded RDT (TgRDT) were estimated as 100% and 97.1% by comparing with ELISA result which uses T. gondii whole cell lysates as the antigen. The TgRDT tested with Uganda people sera for field trial and showed 31.9% of seroprevalence against T. gondii antibody. The TgRDT is proved to be a kit for rapid and easy to use with high accuracy, which would be a suitable serodiagnostic tool for toxoplasmosis.

Citations

Citations to this article as recorded by

Development of an Immunochromatographic Test with Recombinant MIC2-MIC3 Fusion Protein for Serological Detection of Toxoplasma gondii
Jianzhong Wang, Yi Zhao, Jicheng Qiu, Jing Liu, Rui Zhou, Xialin Ma, Xiaojie Wu, Xiaoguang Li, Wei Mao, Yiduo Liu, Heng Zhang
Veterinary Sciences.2025; 12(6): 509. CrossRef
Application of gold immunochromatographic assay strip combined with digital evaluation for early detection of Toxoplasma gondii infection in multiple species
Jiyuan Fan, Hao Sun, Jiawen Fang, Yafan Gao, Haojie Ding, Bin Zheng, Qingming Kong, Xunhui Zhuo, Shaohong Lu
Parasites & Vectors.2024;[Epub] CrossRef
Single Cell Expression Systems for the Production of Recombinant Proteins for Immunodiagnosis and Immunoprophylaxis of Toxoplasmosis
Karolina Sołowińska, Lucyna Holec-Gąsior
Microorganisms.2024; 12(8): 1731. CrossRef
Seroprevalence of Toxoplasma gondii infection among patients of a tertiary hospital in Guangzhou, Guangdong province, PR China
Yu-bin Guan, Xiao-xiao Sun, Shao-lian Chen, Xiao-ting Zhu, Zhi-hua Zeng, Han-wei Lu, Hong-mei Feng, Yu Guo, Wen-gong Jiang, Kui Xiong, Xiao-rong Yang, Ho-Woo Nam, Zhao-shou Yang, Pan Li
PLOS ONE.2023; 18(7): e0286430. CrossRef
Past and present seroprevalence and disease burden estimates of Toxoplasma gondii infections in Germany: An appreciation of the role of serodiagnostics
Frank Seeber
International Journal of Medical Microbiology.2023; 313(6): 151592. CrossRef
Seroprevalence of Toxoplasma gondii assayed using Rapid Diagnostic Tests among Residents in Three Counties Adjacent to The Demilitarized Zone, Korea
Jeehi Jung, Jinyoung Lee, Yoon Kyung Chang, Seong Kyu Ahn, Seo Hye Park, Sung-Jong Hong, Jihoo Lee, Chom-Kyu Chong, Hye-Jin Ahn, Ho-Woo Nam, Tong-Soo Kim, Dongjae Kim
The Korean Journal of Parasitology.2021; 59(1): 9. CrossRef
Clusters of Toxoplasmosis in Ganghwa-gun, Cheorwon-gun, and Goseong-gun, Korea
Jihye Yu, Woojin Kim, Yoon Kyung Chang, Tong-Soo Kim, Sung-Jong Hong, Hye-Jin Ahn, Ho-Woo Nam, Dongjae Kim
The Korean Journal of Parasitology.2021; 59(3): 251. CrossRef
Serological and molecular rapid diagnostic tests for Toxoplasma infection in humans and animals
Amjad Hayat Khan, Rahmah Noordin
European Journal of Clinical Microbiology & Infectious Diseases.2020; 39(1): 19. CrossRef
Clusters of Toxoplasmosis in Gyodong-Myeon and Samsan-Myeon, Ganghwa-Gun, Korea
Woojin Kim, Yoon Kyung Chang, Tong-Soo Kim, Sung-Jong Hong, Hye-Jin Ahn, Ho-Woo Nam, Dongjae Kim
The Korean Journal of Parasitology.2020; 58(5): 493. CrossRef
Identification of novel antigens for serum IgG diagnosis of human toxoplasmosis
Juntao Luo, Jingyi Wan, Ziru Tang, Shuang Shen
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Seroprevalence of Toxoplasmosis with ELISA and Rapid Diagnostic Test among Residents in Gyodong-do, Inchon city, Korea: A Four-Year Follow-up
Yeong Hoon Kim, Ji hoo Lee, Seong kyu Ahn, Tong-Soo Kim, Sung-Jong Hong, Chom-Kyu Chong, Hye-Jin Ahn, Ho-Woo Nam
The Korean Journal of Parasitology.2017; 55(3): 247. CrossRef
Development of direct assays for Toxoplasma gondii and its use in genomic DNA sample
Lívia M. Alves, Vinícius R. Rodovalho, Ana C.H. Castro, Márcia A.R. Freitas, Caroline M. Mota, Tiago W.P. Mineo, José R. Mineo, João M. Madurro, Ana G. Brito-Madurro
Journal of Pharmaceutical and Biomedical Analysis.2017; 145: 838. CrossRef
Seroprevalence of Toxoplasmosis Detected by RDT in Residents near the DMZ (demilitarized zone) of Cheorwon-gun, Gangwon-do, Korea
Yeong Hoon Kim, Jihoo Lee, Young-Eun Kim, Seongkyu Ahn, Tong-Soo Kim, Sung-Jong Hong, Chom-Kyu Chong, Hye-Jin Ahn, Ho-Woo Nam
The Korean Journal of Parasitology.2017; 55(4): 385. CrossRef
Western Blot Detection of Human Anti-Chikungunya Virus Antibody with Recombinant Envelope 2 Protein
Zhaoshou Yang, Jihoo Lee, Hye-Jin Ahn, Chom-Kyu Chong, Ronaldo F. Dias, Ho-Woo Nam
The Korean Journal of Parasitology.2016; 54(2): 239. CrossRef
Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013)
Shelly DeForte, Krishna D Reddy, Vladimir N Uversky
Intrinsically Disordered Proteins.2015; 3(1): e984569. CrossRef
Probability of Antibody Formation against Circumsporozoite Protein of Plasmodium vivax among Korean Malaria Patients
Ho-Woo Nam, Kyoung Ju Song, Hye Jin Ahn, Zhaoshou Yang, Chom-Kyu Chong, Pyo Yun Cho, Seong Kyu Ahn, Tong-Soo Kim
The Korean Journal of Parasitology.2014; 52(2): 143. CrossRef
High Expression of Water-Soluble Recombinant Antigenic Domains ofToxoplasma gondii Secretory Organelles
Zhaoshou Yang, Hye-Jin Ahn, Ho-Woo Nam
The Korean Journal of Parasitology.2014; 52(4): 367. CrossRef

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Real-Time RT-PCR on SAG1 and BAG1 Gene Expression during Stage Conversion in Immunosuppressed Mice Infected with Toxoplasma gondii Tehran Strain: Monavar Selseleh, Mohammad Hossein Modarressi, Mehdi Mohebali, Saeedeh Shojaee, Mohammad Reza Eshragian, Mina Selseleh, Ebrahim Azizi, Hossein Keshavarz; Korean J Parasitol 2012;50(3):199-205.
Published online August 13, 2012; DOI: https://doi.org/10.3347/kjp.2012.50.3.199

Abstract
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Toxoplasmic encephalitis is caused by reactivation of bradyzoites to rapidly dividing tachyzoites of the apicomplexan parasite Toxoplasma gondii in immunocompromised hosts. Diagnosis of this life-threatening disease is problematic, because it is difficult to discriminate between these 2 stages. Toxoplasma PCR assays using gDNA as a template have been unable to discriminate between an increase or decrease in SAG1 and BAG1 expression between the active tachyzoite stage and the latent bradyzoite stage. In the present study, real-time RT-PCR assay was used to detect the expression of bradyzoite (BAG1)- and tachyzoite-specific genes (SAG1) during bradyzoite/tachyzoite stage conversion in mice infected with T. gondii Tehran strain after dexamethasone sodium phosphate (DXM) administration. The conversion reaction was observed in the lungs and brain tissues of experimental mice, indicated by SAG1 expression at day 6 after DXM administration, and continued until day 14. Bradyzoites were also detected in both organs throughout the study; however, it decreased at day 14 significantly. It is suggested that during the reactivation period, bradyzoites not only escape from the cysts and reinvade neighboring cells as tachyzoites, but also converted to new bradyzoites. In summary, the real-time RT-PCR assay provided a reliable, fast, and quantitative way of detecting T. gondii reactivation in an animal model. Thus, this method may be useful for diagnosing stage conversion in clinical specimens of immunocompromised patients (HIV or transplant patients) for early identification of tachyzoite-bradyzoite stage conversion.

Citations

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Human Retinal Organoid Model of Ocular Toxoplasmosis
Liam M. Ashander, Grace E. Lidgerwood, Amanda L. Lumsden, João M. Furtado, Alice Pébay, Justine R. Smith
Pathogens.2025; 14(3): 286. CrossRef
Comprehensive diagnostic approaches to feline toxoplasmosis: Bridging traditional methods and emerging technologies
Dan Zhao, Yanzhen Liao, Hao Liu, Jianwei Wang, Ruiying Liang, Rongqiong Zhou, Jiabo Ding, Sixin Zhang, Xinming Tang
Virulence.2025;[Epub] CrossRef
High Efficacy of Green Synthesized Silver Nanoparticles for Treatment of Toxoplasma Gondii Infection Through Their Immunomodulatory, Anti-Inflammatory, and Antioxidant Potency
Qais A.H. Majeed, Sultan F. Alnomasy, Abdullah F. Shater, Abdullah D. Alanazi
Acta Parasitologica.2024; 69(2): 1201. CrossRef
Diagnosis of Toxoplasmosis Using Surface Antigen Grade 1 Detection by ELISA, Nano-Gold ELISA, and PCR in Pregnant Women
Nagwa SM Aly, Hye-Sook Kim, Yasmin M Marei, Azza S Elhamshary, Ibrahim R Bayoumi, Rabab E Omar, Dina A Mohammed, Shin-Ichi Miyoshi, Gehan A Rashed
International Journal of Nanomedicine.2023; Volume 18: 1335. CrossRef
Assessment of tissue levels of miR-146a and proinflammatory cytokines in experimental cerebral toxoplasmosis following atovaquone and clindamycin treatment: An in vivo study
Nima Zouei, Abdolhossein Dalimi, Majid Pirestani, Fatemeh Ghaffarifar
Microbial Pathogenesis.2023; 184: 106340. CrossRef
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Emily L. Lilly, Nathan J. Webster
Food Microbiology.2021; 99: 103798. CrossRef
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Sanaz Jafarpour Azami, Amir Amani, Hossein Keshavarz, Roqya Najafi-Taher, Mehdi Mohebali, Mohammad Ali Faramarzi, Mahmood Mahmoudi, Saeedeh Shojaee
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ANK1 and DnaK-TPR, Two Tetratricopeptide Repeat-Containing Proteins Primarily Expressed in Toxoplasma Bradyzoites, Do Not Contribute to Bradyzoite Differentiation
Jichao Yang, Lihong Zhang, Huiyan Diao, Ningbo Xia, Yanqin Zhou, Junlong Zhao, Bang Shen
Frontiers in Microbiology.2017;[Epub] CrossRef
Deletion of mitogen-activated protein kinase 1 inhibits development and growth of Toxoplasma gondii
Lili Cao, Zedong Wang, Shuchao Wang, Jiping Li, Xinglong Wang, Feng Wei, Quan Liu
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Brain cystogenesis capacity of Toxoplasma gondii, avirulent Tehran strain in mice
Mehrzad Saraei, Yosef Ghaderi, Tahereh Mosavi, Mojtaba Shahnazi, Hossein Keshavarz, Saeedeh Shojaee
Asian Pacific Journal of Tropical Disease.2014; 4: S739. CrossRef

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Development and Clinical Evaluation of a Rapid Serodiagnostic Test for Toxoplasmosis of Cats Using Recombinant SAG1 Antigen: Chom-Kyu Chong, Wooseog Jeong, Hak-Yong Kim, Dong-Jun An, Hye-Young Jeoung, Jeong-Eun Ryu, A-Ra Ko, Yong-Joo Kim, Sung-Jong Hong, Zhaoshou Yang, Ho-Woo Nam; Korean J Parasitol 2011;49(3):207-212.
Published online September 30, 2011; DOI: https://doi.org/10.3347/kjp.2011.49.3.207

Abstract
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Rapid serodiagnostic methods for Toxoplasma gondii infection in cats are urgently needed for effective control of transmission routes toward human infections. In this work, 4 recombinant T. gondii antigens (SAG1, SAG2, GRA3, and GRA6) were produced and tested for the development of rapid diagnostic test (RDT). The proteins were expressed in Escherichia coli, affinity-purified, and applied onto the nitrocellulose membrane of the test strip. The recombinant SAG1 (rSAG1) showed the strongest antigenic activity and highest specificity among them. We also performed clinical evaluation of the rSAG1-loaded RDT in 182 cat sera (55 household and 127 stray cats). The kit showed 0.88 of kappa value comparing with a commercialized ELISA kit, which indicated a significant correlation between rSAG1-loaded RDT and the ELISA kit. The overall sensitivity and specificity of the RDT were 100% (23/23) and 99.4% (158/159), respectively. The rSAG1-loaded RDT is rapid, easy to use, and highly accurate. Thus, it would be a suitable diagnostic tool for rapid detection of antibodies in T. gondii-infected cats under field conditions.

Citations

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Parasitology Research.2025;[Epub] CrossRef
Comprehensive diagnostic approaches to feline toxoplasmosis: Bridging traditional methods and emerging technologies
Dan Zhao, Yanzhen Liao, Hao Liu, Jianwei Wang, Ruiying Liang, Rongqiong Zhou, Jiabo Ding, Sixin Zhang, Xinming Tang
Virulence.2025;[Epub] CrossRef
Evaluation of an immunochromatographic serologic test to detect the presence of anti‐Toxoplasma gondii antibodies in cats
Sergio Villanueva‐Saz, Mariví Martínez, Jacobo Giner, María Dolores Pérez, Ana Pilar Tobajas, Andrés Yzuel, María Teresa Verde, Delia Lacasta, Antonio Fernández, Diana Marteles, Héctor Ruíz
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A preliminary study to develop a lateral flow assay using recombinant GRA1 protein for the diagnosis of toxoplasmosis in stray cats
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Comparative Immunology, Microbiology and Infectious Diseases.2023; 101: 102057. CrossRef
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Eukote Suwan, Piangjai Chalermwong, Rucksak Rucksaken, Metita Sussadee, Sarawan Kaewmongkol, Ruenruetai Udonsom, Sathaporn Jittapalapong, Bandid Mangkit
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European Journal of Clinical Microbiology & Infectious Diseases.2020; 39(1): 19. CrossRef
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J.P. Dubey, C.K. Cerqueira-Cézar, F.H.A. Murata, O.C.H. Kwok, Y.R. Yang, C. Su
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Benedikt T. Fabian, Fatima Hedar, Martin Koethe, Berit Bangoura, Pavlo Maksimov, Franz J. Conraths, Isabelle Villena, Dominique Aubert, Frank Seeber, Gereon Schares
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Latex–protein complexes from an acute phase recombinant antigen of Toxoplasma gondii for the diagnosis of recently acquired toxoplasmosis
Leandro E. Peretti, Verónica D.G. Gonzalez, Iván S. Marcipar, Luis M. Gugliotta
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A Rapid Diagnostic Test for Toxoplasmosis using Recombinant Antigenic N-terminal Half of SAG1 Linked with Intrinsically Unstructured Domain of GRA2 Protein
Kyoung Ju Song, Zhaoshou Yang, Chom-Kyu Chong, Jin-Soo Kim, Kyung Chan Lee, Tong-Soo Kim, Ho-Woo Nam
The Korean Journal of Parasitology.2013; 51(5): 503. CrossRef
Evaluation of an indirect ELISA using a tachyzoite surface antigen SAG1 for diagnosis of Toxoplasma gondii infection in cats
M. Hosseininejad
Experimental Parasitology.2012; 132(4): 556. CrossRef

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Brief Communication

A role of carboxy-terminal region of Toxoplasma gondii-heat shock protein 70 in enhancement of T. gondii infection in mice: Hye-Seong Mun, Kazumi Norose, Fumie Aosai, Mei Chen, Akihiko Yano; Korean J Parasitol 2000;38(2):107-110.
Published online June 30, 2000; DOI: https://doi.org/10.3347/kjp.2000.38.2.107

Abstract
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We investigated the role of recombinant Toxoplasma gondii heat shock protein (rT.g.HSP) 70-full length, rT.g.HSP70-NH2-terminal region, or rT.g.HSP70-carboxy-terminal region in prophylactic immunity in C57BL/6 mice perorally infected with Fukaya cysts of T. gondii. At 3, 4, 5, and 6 weeks after infection, the number of T. gondii in the brain tissue of each mouse was measured by quantitative competitive-polymerase chain reaction (QC-PCR) targeting the surface antigen (SAG) 1 gene. Immunization with rT.g.HSP70-full length or rT.g.HSP70-carboxy-terminal region increased the number of T.gondii in the brain tissue after T. gondii infection, whereas immunization with rT.g.HSP70-NH₂-terminal region did not. These results suggest that T.g.HSP70-carboxy-terminal region as well as T.g.HSP70-full length may induce deleterious effects on the protective immunity of mice infected with a cyst-forming T. gondii strain, Fukaya.

Citations

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Recombinant TgHSP70 Immunization Protects against Toxoplasma gondii Brain Cyst Formation by Enhancing Inducible Nitric Oxide Expression
Paulo Czarnewski, Ester C. B. Araújo, Mário C. Oliveira, Tiago W. P. Mineo, Neide M. Silva
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