Affinage · Plasmodium

PF3D7_1461300

40S ribosomal protein S28e, putative

Annotated
2026-09-08
5 papers in source corpus 3 papers cited in narrative 3 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1461300 (S28e) is annotated as a component of the small (40S) subunit of the P. falciparum 80S ribosome, established solely through cryo-EM and cryo-electron tomography of the intact ribosome in which S28e is placed as one of the 40S subunit proteins (PMID:24913268, PMID:26432834, PMID:40825879). These structures resolved the 40S subunit in the context of drug interaction — emetine binding the E-site to block mRNA/tRNA translocation (PMID:24913268) — and in native, actively translating states within infected erythrocytes (PMID:40825879), but no finding in the available corpus is uniquely attributed to S28e itself. Beyond its membership in the 40S small subunit complex, no molecular function, interaction, substrate, localization, or modification specific to PF3D7_1461300 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 3 steps
  1. 2014 Low

    The first high-resolution structure of the P. falciparum 80S ribosome placed the 40S small subunit proteins, including S28e, within the assembled ribosome and in the context of antimalarial drug binding, establishing the structural setting in which S28e resides.

    Evidence Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome bound to emetine

    PMID:24913268

    Open questions at the time
    • No finding uniquely attributed to S28e beyond membership in the 40S subunit
    • No S28e-specific interactions, function, or modification defined
    • Emetine binds the E-site, not S28e directly
  2. 2015 Low

    Sub-nanometer cryo-EM reconstructions from blood-stage schizonts refined the atomic model of the malarial 40S subunit and highlighted features distinguishing it from mammalian ribosomes, extending the structural context of S28e as a 40S component.

    Evidence Cryo-EM with flexible-fitting atomic model building from P. falciparum schizont ribosomes

    PMID:26432834

    Open questions at the time
    • No specific structural or functional role assigned to S28e
    • Divergence from mammalian ribosome not localized to S28e
  3. 2025 Low

    In situ cryo-electron tomography captured the native malarial ribosome in actively translating states inside infected erythrocytes and monitored responses to a Plasmodium-specific translation inhibitor, situating the 40S subunit (and thus S28e) in its cellular translational context.

    Evidence In situ cryo-electron tomography of P. falciparum-infected human erythrocytes with drug perturbation

    PMID:40825879

    Open questions at the time
    • No finding specific to S28e distinct from the whole 40S subunit
    • Drug effect described for ribosome states generally, not S28e
    • No S28e-level dynamics resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether S28e has any function, interaction, or property distinct from its structural membership in the 40S subunit remains entirely uncharacterized in the available corpus.
  • No S28e-specific molecular function established
  • No interactors or modifications of S28e reported
  • No genetic or biochemical perturbation of S28e alone

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
40S small ribosomal subunit (P. falciparum)Pf80S ribosome

Evidence

Reading pass · 3 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution was determined, revealing the architecture of the small (40S) subunit, within which S28e (PF3D7_1461300) resides as a component of the ribosomal small subunit. The structure established that emetine binds the E-site of the small subunit to block mRNA/tRNA translocation, placing the 40S subunit proteins including S28e in the context of drug interaction at the ribosome. Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine eLife Low 24913268
2015 Multiple cryo-EM reconstructions of P. falciparum 80S ribosomes purified from blood-stage schizonts at sub-nanometer resolution established structural and dynamic features of the ribosome (including the 40S small subunit, of which S28e/PF3D7_1461300 is a component) that differentiate it from mammalian ribosomes; atomic models were built by flexible fitting into the density maps. Cryo-EM with atomic model building by flexible fitting from P. falciparum blood-stage schizont ribosomes Nucleic acids research Low 26432834
2025 In situ cryo-electron tomography of P. falciparum-infected erythrocytes yielded eight high-resolution structures of the native malarial ribosome in actively translating states, providing molecular-resolution views of the 40S small subunit (which contains S28e/PF3D7_1461300) within the native cellular context; following treatment with a Plasmodium-specific translation inhibitor, elongation factor-bound ribosomal states decreased and apparent ribosome biogenesis was upregulated. In situ cryo-electron tomography of P. falciparum-infected human erythrocytes; drug perturbation experiments Nature structural & molecular biology Low 40825879

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. eLife 272 24913268
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 45 26432834
2010 Assessing functional annotation transfers with inter-species conserved coexpression: application to Plasmodium falciparum. BMC genomics 12 20078859
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 7 40825879
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 3 40480224