Characterization of the Plasmodium vivax erythrocytic stage proteome and identification of a potent immunogenic antigen of the asexual stages
© Roobsoong et al; licensee BioMed Central Ltd. 2010
Published: 20 October 2010
With the genome of Plasmodium vivax sequenced , it would be important to determine proteomes of the parasite in order to assist efforts in understanding the basic biology of the parasite as well as provides the new tools for identifying novel antigens and drug targets.
Materials and methods
Lysates of P. vivax were separated by SDS-polycrylamide gel electrophoresis (SDS-PAGE) and proteins were identified by using matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF/TOF) mass spectrometry. In addition, to identify proteins that might be recognized by host humoral immunity, we have separated them by two-dimensional gel electrophoresis. Proteins were then screened by western blot with immune serum. Spots that were recognized by the host serum were excised and identified by high-accuracy liquid chromatography-tandem mass spectrometry (LC-MS/MS).
Functional classes of all identified proteins.
Protein with binding function
The PV180L encodes a 24.1 kDa hypothetical protein which expressed throughout the erythrocytic cycle of P. vivax and the antibodies to PV180L were long lasting. Therefore, more reports on the proteins of P. vivax parasite provide useful information and availability to facilitate not only basic research on this extraordinary malaria parasite, but also provide the new tools for drug and vaccine developments.
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