A cascade of DNA-binding proteins for sexual commitment and development in Plasmodium

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Sinha, Abhinav and Hughes, Katie R. and Modrzynska, Katarzyna K. and Otto, Thomas D. and Pfander, Claudia and Dickens, Nicholas J. and Religa, Agnieszka A. and Bushell, Ellen and Graham, Anne L. and Cameron, Rachael and Kafsack, Bjorn F. C. and Williams, April E. and Llinás, Manuel and Berriman, Matthew and Billker, Oliver and Waters, Andrew P. (2014) A cascade of DNA-binding proteins for sexual commitment and development in Plasmodium. Nature, 507 (7491). 253–257. ISSN 0028-0836 (https://doi.org/10.1038/nature12970)

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Abstract

Commitment to and completion of sexual development are essential for malaria parasites (protists of the genus Plasmodium) to be transmitted through mosquitoes. The molecular mechanism(s) responsible for commitment have been hitherto unknown. Here we show that PbAP2-G, a conserved member of the apicomplexan AP2 (ApiAP2) family of DNA-binding proteins, is essential for the commitment of asexually replicating forms to sexual development in Plasmodium berghei, a malaria parasite of rodents. PbAP2-G was identified from mutations in its encoding gene, PBANKA_143750, which account for the loss of sexual development frequently observed in parasites transmitted artificially by blood passage. Systematic gene deletion of conserved ApiAP2 genes in Plasmodium confirmed the role of PbAP2-G and revealed a second ApiAP2 member (PBANKA_103430, here termed PbAP2-G2) that significantly modulates but does not abolish gametocytogenesis, indicating that a cascade of ApiAP2 proteins are involved in commitment to the production and maturation of gametocytes. The data suggest a mechanism of commitment to gametocytogenesis in Plasmodium consistent with a positive feedback loop involving PbAP2-G that could be exploited to prevent the transmission of this pernicious parasite.

  • Item type:Article
    ID code:54074
    Dates:
    Date
    Event
    13 March 2014
    Published
    19 December 2013
    Accepted
    Subjects:Science > Chemistry
    Department:Faculty of Science > Pure and Applied Chemistry
    Depositing user: Pure Administrator
    Date deposited:25 Aug 2015 15:44
    Last modified:25 Nov 2024 06:48
    URI:https://strathprints.strath.ac.uk/id/eprint/54074
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