Mitochondrial ATP synthase is dispensable in blood-stage Plasmodium berghei rodent malaria but essential in the mosquito phase

Proc Natl Acad Sci U S A. 2015 Aug 18;112(33):10216-23. doi: 10.1073/pnas.1423959112. Epub 2015 Mar 23.

Abstract

Mitochondrial ATP synthase is driven by chemiosmotic oxidation of pyruvate derived from glycolysis. Blood-stage malaria parasites eschew chemiosmosis, instead relying almost solely on glycolysis for their ATP generation, which begs the question of whether mitochondrial ATP synthase is necessary during the blood stage of the parasite life cycle. We knocked out the mitochondrial ATP synthase β subunit gene in the rodent malaria parasite, Plasmodium berghei, ablating the protein that converts ADP to ATP. Disruption of the β subunit gene of the ATP synthase only marginally reduced asexual blood-stage parasite growth but completely blocked mouse-to-mouse transmission via Anopheles stephensi mosquitoes. Parasites lacking the β subunit gene of the ATP synthase generated viable gametes that fuse and form ookinetes but cannot progress beyond this stage. Ookinetes lacking the β subunit gene of the ATP synthase had normal motility but were not viable in the mosquito midgut and never made oocysts or sporozoites, thereby abrogating transmission to naive mice via mosquito bite. We crossed the self-infertile ATP synthase β subunit knockout parasites with a male-deficient, self-infertile strain of P. berghei, which restored fertility and production of oocysts and sporozoites, which demonstrates that mitochondrial ATP synthase is essential for ongoing viability through the female, mitochondrion-carrying line of sexual reproduction in P. berghei malaria. Perturbation of ATP synthase completely blocks transmission to the mosquito vector and could potentially be targeted for disease control.

Keywords: ATP synthase; aerobic respiration; malaria; mitochondrial endosymbiosis; ookinetes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / chemistry
  • Adenosine Triphosphate / chemistry
  • Animals
  • Bacterial Proteins / metabolism
  • Computational Biology
  • Crosses, Genetic
  • Culicidae
  • Female
  • Gene Expression Regulation, Enzymologic*
  • Glycolysis
  • Luminescent Proteins / metabolism
  • Malaria / parasitology*
  • Male
  • Mice
  • Mitochondria / enzymology*
  • Mitochondrial Proton-Translocating ATPases / metabolism*
  • Oocysts / enzymology
  • Oxygen / chemistry
  • Phenotype
  • Plasmodium berghei / enzymology*
  • Plasmodium berghei / pathogenicity
  • Sporozoites / enzymology
  • Transgenes

Substances

  • Bacterial Proteins
  • Luminescent Proteins
  • yellow fluorescent protein, Bacteria
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Mitochondrial Proton-Translocating ATPases
  • Oxygen