Jiraprapa WipasaChakrit HirunpetcharatYuvadee MahakunkijcharoenHuji XuSalenna ElliottMichael F GoodMahidol University. Faculty of Public Health. Department of Microbiology.Mahidol University. Faculty of Tropical Medicine. Department of Microbiology and Immunology.2013-09-252017-06-272013-09-252017-06-272013-09-262002The Journal of Immunology. Vol.169, No.2 (2002), 944-951https://repository.li.mahidol.ac.th/handle/20.500.14594/2189Merozoite 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.engMahidol UniversityMerozoite surface protein 1T cell epitopesPlasmodium yoeliiBlood stage malaria.Article