Identification of novel rhoptry proteins in Neospora caninum by LC/MS-MS analysis of subcellular fractions

Marugan-Hernandez, V.; Alvarez-Garcia, G.; Tomley, F.; Hemphill, A.; Regidor-Cerrillo, J.; Ortega-Mora, L.M. (2011). Identification of novel rhoptry proteins in Neospora caninum by LC/MS-MS analysis of subcellular fractions. Journal of proteomics, 74(5), pp. 629-42. Amsterdam: Elsevier 10.1016/j.jprot.2011.02.004

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Apicomplexan parasites possess an apical complex that is composed of two secretory organelles recognized as micronemes and rhoptries. Rhoptry contents are secreted into the parasitophorous vacuole during the host cell invasion process. Several rhoptry proteins have been identified in Toxoplasma gondii and seem to be involved in host-pathogen interactions and some of them are considered to be important virulence factors. Only one rhoptry protein, NcROP2, has been identified and extensively characterized in the closely related parasite Neospora caninum, and this has showed immunoprotective properties. Thus, with the aim of increasing knowledge of the rhoptry protein repertoire in N. caninum, a subcellular fractionation of tachyzoites was performed to obtain fractions enriched for this secretory organelle. 2-D SDS-PAGE followed by MS and LC/MS-MS were applied for fraction analysis and 8 potential novel rhoptry components (NcROP1, 5, 8, 30 and NcRON2, 3, 4, 8) and several kinases, proteases and phosphatases proteins were identified with a high homology to those previously found in T. gondii. Their existence in N. caninum tachyzoites suggests their involvement in similar events or pathways that occur in T. gondii. These novel proteins may be considered as targets that could be useful in the future development of immunoprophylactic measures.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Parasitology

UniBE Contributor:

Hemphill, Andrew

ISSN:

1874-3919

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:31

Last Modified:

21 Jan 2014 15:05

Publisher DOI:

10.1016/j.jprot.2011.02.004

Web of Science ID:

000290132700006

URI:

https://boris.unibe.ch/id/eprint/12103 (FactScience: 218384)

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