Proteomic analysis of Toxoplasma gondii KI-1 tachyzoites

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dc.contributor.authorS H Choi-
dc.contributor.authorT Y Kim-
dc.contributor.authorSung Goo Park-
dc.contributor.authorG H Cha-
dc.contributor.authorD W Shin-
dc.contributor.authorJ Y Chai-
dc.contributor.authorY H Lee-
dc.date.accessioned2017-04-19T09:19:39Z-
dc.date.available2017-04-19T09:19:39Z-
dc.date.issued2010-
dc.identifier.issn0023-4001-
dc.identifier.uri10.3347/kjp.2010.48.3.195ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9722-
dc.description.abstractWe 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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleProteomic analysis of Toxoplasma gondii KI-1 tachyzoites-
dc.title.alternativeProteomic analysis of Toxoplasma gondii KI-1 tachyzoites-
dc.typeArticle-
dc.citation.titleKorean Journal of Parasitology-
dc.citation.number3-
dc.citation.endPage201-
dc.citation.startPage195-
dc.citation.volume48-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName최시환-
dc.contributor.alternativeName김태윤-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName차광호-
dc.contributor.alternativeName신대환-
dc.contributor.alternativeName채종일-
dc.contributor.alternativeName이영하-
dc.identifier.bibliographicCitationKorean Journal of Parasitology, vol. 48, no. 3, pp. 195-201-
dc.identifier.doi10.3347/kjp.2010.48.3.195-
dc.subject.keywordKorean isolate-1 (ki-1)-
dc.subject.keywordProteomics-
dc.subject.keywordQuantitative real time pcr-
dc.subject.keywordToxoplasma gondii-
dc.subject.localKorean isolate-1 (ki-1)-
dc.subject.localProteomic-
dc.subject.localProteomics-
dc.subject.localQuantitative real time pcr-
dc.subject.localToxoplasma gondii-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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