Affinage · Plasmodium

RPS15

PF3D7_1358800 · 40S ribosomal protein S15

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1358800 (RPS15) is a structural component of the small (40S) subunit of the Plasmodium falciparum 80S ribosome, established through high-resolution cryo-EM of the intact ribosome (PMID:24913268) and confirmed in native, actively translating ribosomes imaged in situ within infected erythrocytes by cryo-electron tomography (PMID:40825879). Its assignment as a 40S constituent is consistent across multiple independent structural reconstructions from blood-stage parasites, which also delineate features distinguishing the P. falciparum ribosome from its mammalian counterpart (PMID:26432834). Beyond this membership in the 40S small subunit, no enzymatic activity, RPS15-specific binding partners, or direct functional experiments on PF3D7_1358800 itself have been characterized in the available corpus; the emetine E-site block (PMID:24913268) and translation-inhibitor perturbations (PMID:40825879) reported in these studies concern the ribosome as a whole rather than RPS15 specifically.

Mechanistic history

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

    Establishing which proteins build the P. falciparum small ribosomal subunit was needed to define the parasite translation machinery; cryo-EM placed RPS15 as a structural constituent of the 40S subunit.

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

    PMID:24913268

    Open questions at the time
    • No RPS15-specific functional mutagenesis performed
    • Emetine binding maps to the small-subunit E-site, not to RPS15 itself
    • No RPS15-unique binding partners identified
  2. 2015 Medium

    Whether RPS15 assignment held across independent reconstructions and how the parasite 40S differs from the mammalian one was addressed by multiple blood-stage schizont structures, confirming RPS15 membership and parasite-specific ribosomal features.

    Evidence Sub-nanometer cryo-EM with atomic model building by flexible fitting; five reconstructions from blood-stage schizonts

    PMID:26432834

    Open questions at the time
    • RPS15-specific functional role not tested
    • Structural features attributed to the ribosome, not resolved to RPS15 function
    • Single lab
  3. 2025 Medium

    Whether RPS15 is part of the 40S subunit in the physiological cellular context of actively translating ribosomes was confirmed by in situ cryo-ET inside infected erythrocytes.

    Evidence In situ cryo-electron tomography of P. falciparum-infected human erythrocytes; eight high-resolution native translating-state structures

    PMID:40825879

    Open questions at the time
    • No RPS15-specific functional dissection
    • Translation-inhibitor effects observed at the level of whole-ribosome states and biogenesis, not RPS15
    • No RPS15-specific interaction or activity resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether PF3D7_1358800 has any function or interaction distinct from its role as a 40S structural subunit remains unaddressed in the corpus.
  • No RPS15-specific knockdown, knockout, or complementation
  • No RPS15-unique binding partners or extraribosomal activity characterized
  • No enzymatic activity assigned

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
40S small ribosomal subunit of the P. falciparum 80S 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 revealed that RPS15 (40S ribosomal protein S15, PF3D7_1358800) is a component of the small (40S) ribosomal subunit; the structure showed emetine binding at the E-site of the small subunit, blocking mRNA/tRNA translocation. Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine eLife Medium 24913268
2015 Sub-nanometer cryo-EM reconstructions of P. falciparum 80S ribosomes from blood-stage schizonts, with atomic model building by flexible fitting, confirmed RPS15 as a structural constituent of the 40S small subunit and revealed structural/dynamic features differentiating the P. falciparum ribosome from mammalian ribosomes. Cryo-EM at sub-nanometer resolution with atomic model building by flexible fitting; five reconstructions from blood-stage schizonts Nucleic acids research Medium 26432834
2025 Eight high-resolution in situ cryo-electron tomography structures of the native P. falciparum 80S ribosome in actively translating states inside infected erythrocytes confirmed RPS15 as part of the 40S subunit in the physiological cellular context; perturbation with a Plasmodium-specific translation inhibitor decreased elongation factor-bound ribosomal states and appeared to upregulate ribosome biogenesis. In situ cryo-electron tomography of P. falciparum-infected human erythrocytes; eight high-resolution structures of native ribosomes in actively translating states Nature structural & molecular biology Medium 40825879

Source papers

Stage 0 corpus · 4 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 276 24913268
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 46 26432834
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 10 40825879
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 4 40480224