Publication: Identification of T cell epitopes on the 33-kDA fragment of plasmodium yoelii merozoite surface protein 1 and their antibody-independent protective role in immunity to blood stage malaria
Issued Date
2002
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eng
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Mahidol University
Bibliographic Citation
The Journal of Immunology. Vol.169, No.2 (2002), 944-951
Suggested Citation
Jiraprapa Wipasa, Chakrit Hirunpetcharat, Yuvadee Mahakunkijcharoen, Huji Xu, Salenna Elliott, Michael F Good Identification of T cell epitopes on the 33-kDA fragment of plasmodium yoelii merozoite surface protein 1 and their antibody-independent protective role in immunity to blood stage malaria. The Journal of Immunology. Vol.169, No.2 (2002), 944-951. Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/2189
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Title
Identification of T cell epitopes on the 33-kDA fragment of plasmodium yoelii merozoite surface protein 1 and their antibody-independent protective role in immunity to blood stage malaria
Abstract
Merozoite surface protein 1 (MSP1) of malaria parasites undergoes proteolytic processing at least twice before
invasion into a new RBC. The 42-kDa fragment, a product of primary processing, is cleaved by proteolytic enzymes
giving rise to MSP1(33), which is shed from the merozoite surface, and MSP1(19), which is the only fragment carried
into a new RBC. In this study, we have identified T cell epitopes on MSPl (33) of Plasmodium yoelii and have examined
their function in immunity to blood stage malaria. Peptides 20 aa in length, spanning the length of MSP1(33) and
overlapping each other by 10 aa, were analyzed for their ability to induce T cell proliferation in immunized BALB/c and
C57BL/6 mice. Multiple epitopes were recognized by these two strains of mice. Effector functions of the dominant
epitopes were then investigated. Peptides Cm 15 and Cm21 were of particular interest as they were able to induce
effector T cells capable of delaying growth of lethal P. yoelii YM following adoptive transfer into immunodeficient mice
without inducing detectable Ab responses. Homologs of these epitopes could be candidates for inclusion in a subunit
vaccine.