The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria

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 n...

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Main Authors: Morris O. Makobongo, George Riding, Huji Xu, Chakrit Hirunpetcharat, Dianne Keough, John De Jersey, Peter Willadsent, Michael F. Good
Other Authors: Royal Brisbane Hospital
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/21050
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spelling th-mahidol.210502018-07-24T10:30:37Z The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria Morris O. Makobongo George Riding Huji Xu Chakrit Hirunpetcharat Dianne Keough John De Jersey Peter Willadsent Michael F. Good Royal Brisbane Hospital Gehrmann Labs University of Queensland Mahidol University Multidisciplinary 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. 2018-07-24T03:30:37Z 2018-07-24T03:30:37Z 2003-03-04 Article Proceedings of the National Academy of Sciences of the United States of America. Vol.100, No.5 (2003), 2628-2633 10.1073/pnas.0337629100 00278424 2-s2.0-0345701295 https://repository.li.mahidol.ac.th/handle/123456789/21050 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0345701295&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Multidisciplinary
spellingShingle Multidisciplinary
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
description 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.
author2 Royal Brisbane Hospital
author_facet Royal Brisbane Hospital
Morris O. Makobongo
George Riding
Huji Xu
Chakrit Hirunpetcharat
Dianne Keough
John De Jersey
Peter Willadsent
Michael F. Good
format Article
author Morris O. Makobongo
George Riding
Huji Xu
Chakrit Hirunpetcharat
Dianne Keough
John De Jersey
Peter Willadsent
Michael F. Good
author_sort Morris O. Makobongo
title The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
title_short The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
title_full The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
title_fullStr The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
title_full_unstemmed The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
title_sort purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/21050
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