PF3D7_0307200

PF3D7_0307200 (L7) is a structural component of the 60S large subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established through successive high-resolution cryo-EM structures of the parasite ribosome (PMID:24913268, PMID:26432834). It is resolved as an integral large-subunit protein in structures of the ribosome bound to translation-targeting antimalarials, including emetine (PMID:24913268) and (+)-mefloquine (PMID:28288098), and in eight in situ cryo-electron tomography reconstructions of the native, actively translating ribosome inside infected erythrocytes (PMID:40825879). Complexome and thermal-proteome profiling across the intraerythrocytic developmental cycle confirm L7's participation in the 80S ribosome and place it among 60S components exhibiting compositional heterogeneity across blood stages (PMID:37053161, PMID:41315737). Beyond its membership in the 60S large subunit of the P. falciparum ribosome, no experiment in the available corpus has established a specific enzymatic activity, direct binding partner, post-translational modification, or loss-of-function phenotype attributable to L7 itself.

1. 2014 Medium

   The first high-resolution view of the P. falciparum ribosome placed L7 within the 60S subunit, establishing where this protein sits in the cytoplasmic translation machine.

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

   PMID:24913268

   Open questions at the time

   • No functional experiment performed specifically on L7
   • No evidence for L7-specific binding partners beyond ribosomal context
   • No loss-of-function phenotype established
2. 2015 Medium

   Resolving L7 in ribosomes purified from blood-stage schizonts confirmed its membership in the 60S subunit and situated it among structural features distinguishing the parasite ribosome from the mammalian ribosome.

   Evidence Sub-nanometer cryo-EM reconstructions with flexible-fitting atomic modeling of schizont-derived ribosomes

   PMID:26432834

   Open questions at the time

   • L7 role inferred only from complex membership
   • Parasite-specific features not localized to L7 specifically
   • No functional consequence of the structural differences tested for L7
3. 2017 Medium

   A drug-bound structure kept L7 in the 60S subunit while guiding mutagenesis of ribosomal binding-site residues, framing the large subunit in the context of antimalarial mode of action.

   Evidence 3.2 Å cryo-EM of the ribosome bound to (+)-mefloquine with site-directed mutagenesis and structure-guided derivative design

   PMID:28288098

   Open questions at the time

   • Mutagenesis targeted the drug-binding site, not L7 itself
   • No direct role of L7 in drug binding or resistance established
4. 2023 Low

   Analysis of ribosome heterogeneity across the life cycle raised the possibility that 60S components including L7 contribute to stage-specific ribosome specialization.

   Evidence Ribosome profiling and structural analysis reported in a review/analysis of ribosome heterogeneity

   PMID:37053161

   Open questions at the time

   • Abstract does not describe experiments specific to L7
   • Specialization is inferred, not demonstrated functionally for L7
   • No mechanism for stage-specific behavior established
5. 2025 Medium

   In situ cryo-ET of native translating ribosomes and thermal-proteome complexome profiling confirmed L7 as a 60S component within actively elongating ribosomes and tracked its complex participation across blood-stage timepoints.

   Evidence Eight in situ cryo-ET structures in infected erythrocytes [#4] and MAP-X thermal proteome profiling across seven IDC timepoints [#5]

   PMID:40825879 PMID:41315737

   Open questions at the time

   • L7 established only as a large-subunit component of the translating ribosome
   • No L7-specific functional assay in the elongation cycle
   • Dynamic complex changes not resolved to L7-specific behavior

• Whether L7 has any function, interaction, modification, or phenotype beyond its structural membership in the 60S subunit remains unaddressed by the available corpus.
• No L7-specific enzymatic activity or binding partner identified
• No genetic loss-of-function or knockdown of L7
• No post-translational modification characterized for L7