Publication: The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
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2003-03-04
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00278424
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2-s2.0-0345701295
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Mahidol University
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SCOPUS
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Proceedings of the National Academy of Sciences of the United States of America. Vol.100, No.5 (2003), 2628-2633
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Morris O. Makobongo, George Riding, Huji Xu, Chakrit Hirunpetcharat, Dianne Keough, John De Jersey, Peter Willadsent, Michael F. Good The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria. Proceedings of the National Academy of Sciences of the United States of America. Vol.100, No.5 (2003), 2628-2633. doi:10.1073/pnas.0337629100 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/21050
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The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
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Although there is good evidence that Immun. to the blood stages of malaria parasites can be mediated by different effector components of the adaptive immune system, target antigens for a Prin. component, effector CD4+ T cells, have never been defined. We generated CD4+ T cell lines to fractions of native antigens from the blood stages of the rodent parasite, Plasmodium yoelii,/identified fraction-specific T cells that had a Th1 phenotype (producing IL-2, IFN-γ, and tumor necrosis factor-α, but not IL-4, after antigenic stimulation). These T cells could inhibit parasite growth in recipient severe combined immunodeficient mice. N-terminal sequencing of the fraction showed identity with hypoxanthine guanine xanthine phosphoribosyl transferase (HGXPRT). Recombinant HGXPRT from the human malaria parasite, Plasmodium falciparum, activated the T cells in vitro, and immunization of normal mice with recombinant HGXPRT reduced parasite growth rates in all mice after challenge.