Proteomic analysis of the Theileria annulata schizont

Witschi, Marc; Xia, D.; Sanderson, S.; Baumgartner, M.; Wastling, J. M.; Dobbelaere, Dirk, (2013). Proteomic analysis of the Theileria annulata schizont. International journal for parasitology, 43(2), pp. 173-180. Elsevier 10.1016/j.ijpara.2012.10.017

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The apicomplexan parasite, Theileria annulata, is the causative agent of tropical theileriosis, a devastating lymphoproliferative disease of cattle. The schizont stage transforms bovine leukocytes and provides an intriguing model to study host/pathogen interactions. The genome of T. annulata has been sequenced and transcriptomic data are rapidly accumulating. In contrast, little is known about the proteome of the schizont, the pathogenic, transforming life cycle stage of the parasite. Using one-dimensional (1-D) gel LC-MS/MS, a proteomic analysis of purified T. annulata schizonts was carried out. In whole parasite lysates, 645 proteins were identified. Proteins with transmembrane domains (TMDs) were under-represented and no proteins with more than four TMDs could be detected. To tackle this problem, Triton X-114 treatment was applied, which facilitates the extraction of membrane proteins, followed by 1-D gel LC-MS/MS. This resulted in the identification of an additional 153 proteins. Half of those had one or more TMD and 30 proteins with more than four TMDs were identified. This demonstrates that Triton X-114 treatment can provide a valuable additional tool for the identification of new membrane proteins in proteomic studies. With two exceptions, all proteins involved in glycolysis and the citric acid cycle were identified. For at least 29% of identified proteins, the corresponding transcripts were not present in the existing expressed sequence tag databases. The proteomics data were integrated into the publicly accessible database resource at EuPathDB (www.eupathdb.org) so that mass spectrometry-based protein expression evidence for T. annulata can be queried alongside transcriptional and other genomics data available for these parasites.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Research Foci > Host-Pathogen Interaction
05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH) > Molecular Pathobiology
05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH)

UniBE Contributor:

Witschi, Marc and Dobbelaere, Dirk,

Subjects:

600 Technology > 630 Agriculture

ISSN:

0020-7519

Publisher:

Elsevier

Language:

English

Submitter:

Susanne Portner

Date Deposited:

28 Jul 2014 16:01

Last Modified:

14 Oct 2015 11:36

Publisher DOI:

10.1016/j.ijpara.2012.10.017

PubMed ID:

23178997

Uncontrolled Keywords:

Apicomplexa, Detergent, Triton X-114, Mass spectrometry, Proteome, Theileria, Transformation, Transmembrane domain

URI:

https://boris.unibe.ch/id/eprint/43931

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