Comparative proteomic analysis of different Toxoplasma gondii genotypes by two‐dimensional fluorescence difference gel electrophoresis combined with mass spectrometry. Issue 4 (2nd December 2013)
- Record Type:
- Journal Article
- Title:
- Comparative proteomic analysis of different Toxoplasma gondii genotypes by two‐dimensional fluorescence difference gel electrophoresis combined with mass spectrometry. Issue 4 (2nd December 2013)
- Main Title:
- Comparative proteomic analysis of different Toxoplasma gondii genotypes by two‐dimensional fluorescence difference gel electrophoresis combined with mass spectrometry
- Authors:
- Zhou, Dong‐Hui
Zhao, Fu‐Rong
Nisbet, Alasdair J.
Xu, Min‐Jun
Song, Hui‐Qun
Lin, Rui‐Qing
Huang, Si‐Yang
Zhu, Xing‐Quan - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Toxoplasma gondii</italic> is a protozoan parasite infecting almost all warm‐blooded animals and humans. There are three infective stages of <italic>T. gondii</italic>: the tachyzoites, the bradyzoites, and the oocysts. The tachyzoite is a rapidly multiplying stage and the main pathogenic factor. In North America and Europe, <italic>T. gondii</italic> is consisted of four major clonal lineages (namely Types I, II, III, and Type 12). In this study, we explored the proteomic profiles of different genotypes (Type I‐RH strain, Type II‐PRU strain, Type II‐TgQHO strain, and ToxoDB 9‐TgC7 strain) of <italic>T. gondii</italic> tachyzoites by using 2D DIGE combined with MALDI‐TOF MS. Totally, 110 differentially abundant protein spots were selected. Of these, 98 spots corresponding to 56 proteins from <italic>T. gondii</italic> were successfully identified. These included surface antigen (SAG1), heat shock protein 70 (Hsp 70), disulfide isomerase, coronin, heat shock protein 60 (Hsp 60), pyruvate kinase, receptor for activated C kinase 1, and peroxiredoxin. Gene ontology enrichment analysis revealed that most of the differentially abundant proteins were involved in biological regulation, metabolic process, response to stress, binding, antioxidant activity, and transporter activity. According to the KEGG metabolic pathway maps of <italic>T. gondii</italic>, some identified proteins were<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Toxoplasma gondii</italic> is a protozoan parasite infecting almost all warm‐blooded animals and humans. There are three infective stages of <italic>T. gondii</italic>: the tachyzoites, the bradyzoites, and the oocysts. The tachyzoite is a rapidly multiplying stage and the main pathogenic factor. In North America and Europe, <italic>T. gondii</italic> is consisted of four major clonal lineages (namely Types I, II, III, and Type 12). In this study, we explored the proteomic profiles of different genotypes (Type I‐RH strain, Type II‐PRU strain, Type II‐TgQHO strain, and ToxoDB 9‐TgC7 strain) of <italic>T. gondii</italic> tachyzoites by using 2D DIGE combined with MALDI‐TOF MS. Totally, 110 differentially abundant protein spots were selected. Of these, 98 spots corresponding to 56 proteins from <italic>T. gondii</italic> were successfully identified. These included surface antigen (SAG1), heat shock protein 70 (Hsp 70), disulfide isomerase, coronin, heat shock protein 60 (Hsp 60), pyruvate kinase, receptor for activated C kinase 1, and peroxiredoxin. Gene ontology enrichment analysis revealed that most of the differentially abundant proteins were involved in biological regulation, metabolic process, response to stress, binding, antioxidant activity, and transporter activity. According to the KEGG metabolic pathway maps of <italic>T. gondii</italic>, some identified proteins were involved in the glycolytic/gluconeogenesis pathway. The present study identified differentially abundant proteins among different genotypes of <italic>T. gondii</italic> and these findings have implications for the better understanding of the phenotypic differences among the examined <italic>T. gondii</italic> genotypes, which in turn may contribute to the better control of toxoplasmosis.</p> </abstract> … (more)
- Is Part Of:
- Electrophoresis. Volume 35:Issue 4(2014:Feb.)
- Journal:
- Electrophoresis
- Issue:
- Volume 35:Issue 4(2014:Feb.)
- Issue Display:
- Volume 35, Issue 4 (2014)
- Year:
- 2014
- Volume:
- 35
- Issue:
- 4
- Issue Sort Value:
- 2014-0035-0004-0000
- Page Start:
- 533
- Page End:
- 545
- Publication Date:
- 2013-12-02
- Subjects:
- Electrophoresis -- Periodicals
Electrophoresis -- Periodicals
541.372 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1522-2683 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/elps.201300044 ↗
- Languages:
- English
- ISSNs:
- 0173-0835
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3706.378000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3102.xml