Publication: The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
Issued Date
2003-03-04
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ISSN
00278424
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2-s2.0-0345701295
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Mahidol University
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SCOPUS
Bibliographic Citation
Proceedings of the National Academy of Sciences of the United States of America. Vol.100, No.5 (2003), 2628-2633
Suggested Citation
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/20.500.14594/21050
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Title
The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
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Abstract
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.