Affinage · Plasmodium

PF3D7_0516900

60S ribosomal protein L2

Annotated
2026-09-07
10 papers in source corpus 3 papers cited in narrative 3 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0516900 (L2) is a structural constituent of the large 60S subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, resolved as a component of the intact malarial ribosome by cryo-EM (PMID:24913268) and confirmed as part of the natively translating ribosome by in situ cryo-electron tomography inside infected erythrocytes (PMID:40825879). It is also present in heterogeneous ribosome populations across parasite life-cycle stages (PMID:37053161). Beyond its assignment as a 60S subunit component, no specific catalytic or regulatory function has been experimentally characterized for L2 itself in the available corpus.

Mechanistic history

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

    Establishing the subunit composition of the malarial ribosome placed L2 within the 60S large subunit of the intact cytoplasmic 80S ribosome, defining its basic structural membership.

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

    PMID:24913268

    Open questions at the time
    • No functional experiment targets L2 individually
    • No catalytic or regulatory role assigned
    • Does not address stage-specific variation
  2. 2023 Low

    Assessing ribosome heterogeneity across the life cycle tested whether L2 is a constant or variable component, placing it among constituents of heterogeneous 60S subunits in stage-specific ribosome populations.

    Evidence Structural and compositional analysis of stage-specific Plasmodium ribosomes

    PMID:37053161

    Open questions at the time
    • Abstract-level compositional mention without functional characterization of L2
    • Does not establish whether L2 occupancy itself varies
    • No mechanism linking heterogeneity to translation
  3. 2025 Medium

    Resolving the ribosome in its native cellular context confirmed that L2 is a structural component of the 60S subunit within physiologically translating ribosomes, extending the in vitro assignment to actively translating states in situ.

    Evidence In situ cryo-electron tomography of ribosomes inside P. falciparum-infected human erythrocytes, yielding eight high-resolution translating-state structures

    PMID:40825879

    Open questions at the time
    • No functional experiment isolates L2's contribution to translation
    • No structural role for L2 within the subunit is dissected
    • Does not address essentiality or drug targeting of L2

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether L2 has any function beyond serving as a 60S structural component — including essentiality, assembly role, or contribution to ribosome heterogeneity — remains uncharacterized.
  • No gene knockdown/knockout of L2
  • No assembly or biogenesis role established
  • No specific catalytic or regulatory activity assigned

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
60S large ribosomal subunitcytoplasmic 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 L2 (PF3D7_0516900) is a component of the large 60S ribosomal subunit within the intact malarial cytoplasmic ribosome complex bound to emetine. Cryo-EM structure determination at 3.2 Å resolution eLife Medium 24913268
2023 Ribosome heterogeneity studies in Plasmodium parasites place L2 (PF3D7_0516900) as a constituent of the 60S large subunit of heterogeneous ribosome populations across parasite life-cycle stages. Structural and compositional analysis of stage-specific ribosomes PLoS pathogens Low 37053161
2025 In situ cryo-electron tomography of P. falciparum-infected erythrocytes resolved eight high-resolution structures of the native malarial ribosome in actively translating states, establishing that L2 (PF3D7_0516900) is a structural component of the large 60S subunit within the physiologically translating ribosome in its native cellular context. In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes Nature structural & molecular biology Medium 40825879

Source papers

Stage 0 corpus · 10 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
2017 Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis. Nature microbiology 138 28288098
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 46 26432834
2020 Plasmodium falciparum translational machinery condones polyadenosine repeats. eLife 21 32469313
2023 Ribosome heterogeneity and specialization of Plasmodium parasites. PLoS pathogens 14 37053161
2019 Adaptation of Translational Machinery in Malaria Parasites to Accommodate Translation of Poly-Adenosine Stretches Throughout Its Life Cycle. Frontiers in microbiology 12 31866984
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 10 40825879
2021 Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Communications biology 8 34017052
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 4 40480224
2017 Parasite physiology: No longer lost in translation. Nature microbiology 0 28540920