Toxoplasma gondii: Proteomic analysis of antigenicity of soluble tachyzoite antigen

Ma, Guangyuan; Zhang, Jianzhong; Yin, Guangwen; Zhang, Jianhong; Meng, Xiangjun; Zhao, Fei

doi:10.1016/j.exppara.2009.01.011

Cited by 54 publications

(54 citation statements)

References 43 publications

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“…Dlugonska et al [9] resolved more than 200 spots of T. gondii tachyzoite lysates, and identified eleven excretory-secretory dense granule proteins that contained B cell epitopes, as well as 2 containing T cell epitopes. Ma et al [10] reported that 1,227 protein spots of T. gondii soluble tachyzoite antigen were fractionated by 2-DE at a pH range of 3-10, and they identified 426 by mass spectrometric analysis and database searches. Xia et al [11] used 3 complementary approaches (2-DE, gel-liquid chromatography linked tandem mass spectrometry, and MudPIT), and identified nearly one-third (2,252) of all the predicted proteins of T. gondii, with 2,477 intron-spanning peptides providing evidence for correct splice site annotation.…”

Section: Discussionmentioning

confidence: 99%

“…Such analyses can provide information about specificity and virulence, and contribute to the development of therapeutic agents and an effective vaccine. A number of studies based on 2-dimensional electrophoresis (2-DE) and mass spectrometry have been performed on T. gondii [8][9][10][11][12]. For example, Cohen et al [8] characterized global protein expression of the T. gondii RH strain by 2-DE and matrixassisted laser-desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry, while Xia et al [11] analyzed the proteome of 3 strains of Toxoplasma (ME49, GT1, and VEG) using 2-DE, gel liquid chromatography-linked tandem mass spectrometry, and multidimensional protein identification technology (Mud-PIT).…”

Section: Introductionmentioning

confidence: 99%

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Proteomic Analysis ofToxoplasma gondiiKI-1 Tachyzoites

et al. 2010

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Abstract:We studied on the proteomic characteristics of Toxoplasma gondii KI-1 tachyzoites which were originally isolated from a Korean patient, and compared with those of the well-known virulent RH strain using 2-dimensional electrophoresis (2-DE), mass spectrometry, and quantitative real-time PCR. Two-dimensional separation of the total proteins isolated from KI-1 tachyzoites revealed up to 150 spots, of which 121 were consistent with those of RH tachyzoites. Of the remaining 29 spots, 14 showed greater than 5-fold difference in density between the KI-1 and RH tachyzoites at a pH of 5.0-8.0. Among the 14 spots, 5 from the KI-1 isolate and 7 from the RH strain were identified using MALDI-TOF mass spectrometry and database searches. The spots from the KI-1 tachyzoites were dense granule proteins (GRA 2, 3, 6, and 7), hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGRPTase), and uracil phosphoribosyltransferase (UPRTase). The spots from the RH strain were surface antigen 1 (SAG 1), L-lactate dehydrogenase (LDH), actin, chorismate synthase, peroximal catalase, hexokinase, bifunctional dihydrofolate reductase-thymidylate synthase (DHTR-TS), and nucleosidetriphosphatases (NTPases). Quantitative real-time PCR supported our mass spectrometric results by showing the elevated expression of the genes encoding GRA 2, 3, and 6 and UPRTase in the KI-1 tachyzoites and those encoding GRA 7, SAG 1, NTPase, and chorismate synthase in the RH tachyzoites. These observations demonstrate that the protein compositions of KI-1 and RH tachyzoites are similar but differential protein expression is involved in virulence.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis ofToxoplasma gondiiKI-1 Tachyzoites

et al. 2010

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“…gondii heat shock protein 60 (TgHSP60) is a member of the HSP60 subfamily (Toursel et al, 2000), which plays an important role in intracellular survival and in the differentiation of T. gondii and also mediates its virulence (Shonhai et al, 2011). In addition, TgHSP60 not only serves as a signal for the activation of antigen presenting cells by inducing the release of cytokines and stimulation of the initial immune response, but also acts as a molecular chaperone in the mitochondria (Ma et al, 2009). Regardless of the key biological roles of TgHSP60 mentioned above, no previous studies have elucidated the sequence diversity of the HSP60 gene among T. gondii isolates from different origins.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Toxoplasma gondii hsp60 gene sequences from different hosts and geographical locations

et al. 2014

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ABSTRACT. The intracellular protozoan Toxoplasma gondii is one of the most successful parasites, with the ability to invade all warmblooded animals, including humans. T. gondii heat shock protein 60 (TgHSP60) plays an important role in intracellular survival and in the differentiation of the parasite, and is also recognized as being associated with its virulence. In the present study, we examined sequence variation in the hsp60 coding region among five T. gondii isolates from different hosts and geographical regions, which were compared with the corresponding sequences of strains ME49, 76K, and GT1 available in the ToxoDB databases. The length of the T. gondii hsp60 sequence was 1728 bp for all strains, and the A+T content ranged from 41.96 to 42.13%. The sequence alignment of the 8 T. gondii strains identified 20 variable positions (0-1.44%) and showed 1.16% overall sequence 6907 ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 13 (3): 6906-6911 (2014) Sequence variation in the T. gondii hsp60 gene variation, suggesting a relatively considerable sequence diversity. Phylogenetic analysis of hsp60 sequences using Bayesian inference and maximum parsimony differentiated the two major clonal lineage types into their respective clusters, and thus separated atypical strains from classical genotypes. The results of the present study suggested that the coding region of the hsp60 gene may represent a novel genetic marker for intraspecies phylogenetic analyses of T. gondii.

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“…T. gondii-derived HSP70 stimulated maturation of murine marrowderived DCs through TLR4 [60] . Under stress conditions, T. gondii RH strain tachyzoites differentiated into bradyzoites and induced T. gondii HSP70 (TgHSP70) protein expression, a highly immunogenic protein [318][319][320][321] . Also, reactivationTgHSP70 in vivo induced expression of TgHSP70 during bradyzoite to tachyzoite interconversion [322] .…”

Section: T Gondii Infectionmentioning

confidence: 99%

Possible Pivotal Role of Latent Chronic T. gondii Infection in the Pathogenesis of Atherosclerosis

Prandota

2017

Journal of Cardiology and Therapy

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Toxoplasma gondii: Proteomic analysis of antigenicity of soluble tachyzoite antigen

Cited by 54 publications

References 43 publications

Proteomic Analysis ofToxoplasma gondiiKI-1 Tachyzoites

Proteomic Analysis ofToxoplasma gondiiKI-1 Tachyzoites

Characterization of the Toxoplasma gondii hsp60 gene sequences from different hosts and geographical locations

Possible Pivotal Role of Latent Chronic T. gondii Infection in the Pathogenesis of Atherosclerosis

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