| 2002 |
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| 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. |
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| Wipasa, J., Hirunpetcharat, C., Mahakunkijcharoen, Y., Xu, H., Elliott, S., and Good, M. F.
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| Cooperative Research Center for Vaccine Technology, Queensland Institute of Medical Research,
Royal Brisbane Hospital, Queensland, Australia |
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| 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 MSP1(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 Cm15 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 |
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| Published in:J.Immunol. 169[2], 944-951. 15-7-2002. |
