Affinage · Plasmodium

PIC6

PF3D7_0530300 · PhIL1-interacting candidate PIC6

Audit flag: identity unverified
Annotated
2026-09-07
5 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PIC6 (PF3D7_0530300) is a component of the inner membrane complex (IMC) of Plasmodium falciparum, identified through its association with PhIL1 (PMID:33830607). In asexual blood-stage parasites, PIC6 was recovered among previously uncharacterized proteins enriched by PhIL1-BioID proximity labeling, and endogenous GFP-tagging confirmed its localization to the IMC (PMID:33830607). Beyond establishing PIC6 as a PhIL1-proximal IMC protein, no molecular activity, substrate, or functional role for PIC6 itself has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2017 Low

    Before this work it was unknown which proteins associate with PhIL1 in the gametocyte IMC; co-immunoprecipitation placed PIC6 within the PhIL1-associated complex, marking it as a candidate IMC component.

    Evidence Immunoprecipitation followed by mass spectrometry of the gametocyte IMC in P. falciparum

    PMID:28985225

    Open questions at the time
    • Single Co-IP/MS identification without reciprocal validation or direct functional follow-up on PIC6
    • Does not establish whether the interaction is direct or bridged by other complex members
    • No localization confirmation of PIC6 itself in gametocytes
  2. 2021 Medium

    Whether PIC6 is a bona fide IMC resident rather than a transient co-purifying protein was unresolved; proximity labeling plus endogenous tagging established PIC6 as a validated IMC protein in asexual blood stages.

    Evidence PhIL1-BioID proximity-dependent biotinylation with mass spectrometry, plus endogenous GFP-tagging for localization, in asexual blood-stage P. falciparum

    PMID:33830607

    Open questions at the time
    • No functional characterization (knockout/knockdown) of PIC6 to define its role in the IMC
    • Molecular activity and direct binding partners of PIC6 remain undefined
    • No structural model or domain-level mechanism established

Open questions

Synthesis pass · forward-looking unresolved questions
  • The specific molecular function of PIC6 within the IMC, its essentiality, and whether it acts beyond passive complex membership remain unknown.
  • No loss-of-function phenotype reported for PIC6
  • No defined biochemical activity or substrate
  • Role across life-cycle stages beyond IMC association undetermined

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
PhIL1-associated IMC complex

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2021 PIC6 (PF3D7_0530300) was identified as one of nine previously uncharacterized proteins enriched by PhIL1-BioID proximity labeling in asexual blood-stage P. falciparum, and validated as a new IMC protein by endogenous GFP-tagging, confirming its localization to the inner membrane complex. BioID proximity-dependent biotinylation using PhIL1 as bait, followed by mass spectrometry peptide identification and endogenous GFP-tagging for validation Cellular microbiology Medium 33830607
2017 PIC6 (PF3D7_0530300) was identified as a PhIL1-interacting candidate by immunoprecipitation and mass spectrometry of the gametocyte IMC, placing it as a component of the PhIL1-associated IMC complex in gametocytes. Immunoprecipitation followed by mass spectrometry PLoS pathogens Low 28985225

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 Disrupting assembly of the inner membrane complex blocks Plasmodium falciparum sexual stage development. PLoS pathogens 65 28985225
2021 Identification of novel inner membrane complex and apical annuli proteins of the malaria parasite Plasmodium falciparum. Cellular microbiology 33 33830607
2017 Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development. Scientific reports 25 29138437
2021 Plasmodium falciparum PhIL1-associated complex plays an essential role in merozoite reorientation and invasion of host erythrocytes. PLoS pathogens 10 34324609
2024 An inner membrane complex protein IMC1g in Plasmodium berghei is involved in asexual stage schizogony and parasite transmission. mBio 6 39576115