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Phosphorylation of eukaryotic initiation factor-2{alpha} promotes the extracellular survival of obligate intracellular parasite Toxoplasma gondii.


ABSTRACT: While seeking a new host cell, obligate intracellular parasites, such as the protozoan Toxoplasma gondii, must be able to endure the stress of an extracellular environment. The mechanisms Toxoplasma use to remain viable while deprived of a host cell are not understood. We have previously shown that phosphorylation of Toxoplasma eukaryotic initiation factor-2? (TgIF2?) is a conserved response to stress. Here we report the characterization of Toxoplasma harboring a point mutation (S71A) in TgIF2? that prevents phosphorylation. Results show that TgIF2? phosphorylation is critical for parasite viability because the TgIF2?-S71A mutants are ill-equipped to cope with life outside the host cell. The TgIF2?-S71A mutants also showed a significant delay in producing acute toxoplasmosis in vivo. We conclude that the phosphorylation of TgIF2? plays a crucial role during the lytic cycle by ameliorating the stress of the extracellular environment while the parasite searches for a new host cell.

SUBMITTER: Joyce BR 

PROVIDER: S-EPMC2951449 | biostudies-other | 2010 Oct

REPOSITORIES: biostudies-other

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Phosphorylation of eukaryotic initiation factor-2{alpha} promotes the extracellular survival of obligate intracellular parasite Toxoplasma gondii.

Joyce Bradley R BR   Queener Sherry F SF   Wek Ronald C RC   Sullivan William J WJ  

Proceedings of the National Academy of Sciences of the United States of America 20100920 40


While seeking a new host cell, obligate intracellular parasites, such as the protozoan Toxoplasma gondii, must be able to endure the stress of an extracellular environment. The mechanisms Toxoplasma use to remain viable while deprived of a host cell are not understood. We have previously shown that phosphorylation of Toxoplasma eukaryotic initiation factor-2α (TgIF2α) is a conserved response to stress. Here we report the characterization of Toxoplasma harboring a point mutation (S71A) in TgIF2α  ...[more]

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