Affinage · Plasmodium

EIF3M

PF3D7_0418200 · eukaryotic translation initiation factor 3 subunit M, putative

Annotated
2026-09-08
4 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0418200 (EIF3M), a putative eukaryotic translation initiation factor 3 subunit of Plasmodium falciparum, is defined in the available corpus principally by its association with translationally repressed mRNP complexes during blood-stage development (PMID:38702310). It was identified as a component of stress granule-like mRNPs that assemble in nutritionally stressed schizonts, co-purifying with PfDOZI, PABP2, CITH, PAIP1, and the eIF2B complex; notably, it is absent from the PfDOZI-associated granules of gametocytes, indicating stage-specific incorporation into distinct mRNP assemblies (PMID:38702310). EIF3M also carries phosphorylation and 2-hydroxyisobutyrylation marks detected in blood-stage parasites (PMID:33517144). Beyond this complex membership and the presence of these post-translational modifications, no writers, erasers, functional consequences, or independent biochemical activity of PF3D7_0418200 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2020 Low

    Establishing that PF3D7_0418200 is a modified protein during the intraerythrocytic cycle raised the question of whether its function is regulated post-translationally, providing the first molecular handle on the protein.

    Evidence Mass spectrometry-based proteome-wide PTM mapping across intraerythrocytic developmental stages in P. falciparum

    PMID:33517144

    Open questions at the time
    • No writers, erasers, or readers of the phosphorylation or 2-hydroxyisobutyrylation marks were identified for EIF3M
    • No functional consequence of the modifications was tested
    • Single large-scale proteomics screen without targeted validation
  2. 2024 Medium

    Placing PF3D7_0418200 within stress granule-like mRNPs answered where the protein acts, linking it to translational repression machinery under nutritional stress and revealing stage-specific complex composition.

    Evidence Co-immunoprecipitation / quantitative interactome proteomics of PfDOZI under stress conditions in P. falciparum schizonts and gametocytes

    PMID:38702310

    Open questions at the time
    • EIF3M was detected as a component but not individually validated by reciprocal pull-down or mutagenesis
    • Whether EIF3M is required for mRNP assembly, stability, or translational repression is unknown
    • The molecular basis for its exclusion from gametocyte PfDOZI granules is not resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether PF3D7_0418200 performs a canonical eIF3-type translation initiation function, or acts primarily as a stress-responsive mRNP component, remains unresolved.
  • No direct assay of translation initiation activity for EIF3M
  • No genetic knockout or knockdown phenotype reported
  • No structural or reciprocal biochemical validation of its complex associations

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Stress granule-like mRNP containing PfDOZI, PABP2, CITH, PAIP1, and eIF2B (nutritionally stressed schizonts) [#0]

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2024 EIF3M (PF3D7_0418200) was identified as a component of stress granule-like mRNPs in nutritionally stressed P. falciparum schizonts, co-purifying with PfDOZI, PABP2, CITH, PAIP1, and the eIF2B complex, but absent from gametocyte PfDOZI-associated granules, indicating stage-specific incorporation into distinct mRNP complexes. Co-immunoprecipitation / quantitative interactome proteomics of PfDOZI under stress conditions Nature communications Medium 38702310
2020 EIF3M (PF3D7_0418200) undergoes phosphorylation and 2-hydroxyisobutyrylation as post-translational modifications in P. falciparum blood-stage parasites, detected in a proteome-wide PTM profiling study. Mass spectrometry-based proteome-wide PTM mapping across intraerythrocytic developmental stages Molecular & cellular proteomics : MCP Low 33517144

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Differential T-cell responses of semi-immune and susceptible malaria subjects to in silico predicted and synthetic peptides of Plasmodium falciparum. Acta tropica 5 24681218
2025 Covalent inhibition of Plasmodium falciparum Ubc13 impairs global protein synthesis. iScience 0 40491475
2024 The DEAD-box RNA helicase PfDOZI imposes opposing actions on RNA metabolism in Plasmodium falciparum. Nature communications 0 38702310
2020 Protein Modification Characteristics of the Malaria Parasite Plasmodium falciparum and the Infected Erythrocytes. Molecular & cellular proteomics : MCP 0 33517144