Affinage · Plasmodium

PIC2

PF3D7_0822900 · PhIL1-interacting candidate PIC2

Audit flag: identity unverified
Annotated
2026-09-08
5 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PIC2 (PF3D7_0822900) is characterized in the available corpus only as a candidate component of the PhIL1-interacting protein complex associated with the inner membrane complex (IMC) of Plasmodium falciparum, where it was identified by co-immunoprecipitation/mass spectrometry using PhIL1 as bait in gametocytes (PMID:28985225) and independently enriched in a BioID proximity-labeling screen with PhIL1 as bait in asexual blood-stage parasites (PMID:33830607). Beyond this association with the PhIL1 complex, no independent functional, structural, or localization data specific to PIC2 have been characterized in the available corpus.

Mechanistic history

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

    To define the composition of the gametocyte IMC-associated PhIL1 complex, this work asked which proteins physically associate with PhIL1 and identified PIC2 as one of them.

    Evidence Immunoprecipitation of PhIL1 followed by mass spectrometry in P. falciparum gametocytes

    PMID:28985225

    Open questions at the time
    • Single Co-IP/MS experiment with no reciprocal pulldown using PIC2 as bait
    • No functional role established for PIC2 itself
    • No localization or structural data specific to PIC2
  2. 2021 Low

    To test whether the PhIL1 association extends to asexual stages and to corroborate the complex membership by an independent method, proximity labeling asked which proteins are near PhIL1 in blood-stage parasites, again recovering PIC2.

    Evidence BioID proximity-dependent biotin identification with PhIL1 as bait followed by mass spectrometry in asexual blood-stage P. falciparum

    PMID:33830607

    Open questions at the time
    • Proximity enrichment does not demonstrate direct binding to PhIL1
    • No PIC2-specific functional or localization experiment reported
    • Does not resolve whether PIC2 is a stable subunit or a transient neighbor

Open questions

Synthesis pass · forward-looking unresolved questions
  • The intrinsic molecular activity, subcellular localization, and functional contribution of PIC2 to the IMC remain undefined, as all evidence to date derives from PhIL1-centric interaction screens rather than direct study of PIC2.
  • No gene knockout or knockdown phenotype for PIC2
  • No demonstration of direct PhIL1-PIC2 binding versus indirect complex membership
  • No structural model or domain-level functional assignment

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
PHIL1 (BAIT IN CO-IP/MS AND BIOID; PIC2 IDENTIFIED AS INTERACTING CANDIDATE)
Complex memberships
PhIL1-interacting protein complex (IMC-associated)

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 PIC2 (PF3D7_0822900) was identified as a component of the PhIL1-interacting protein complex in the gametocyte inner membrane complex (IMC) of P. falciparum, revealed by immunoprecipitation of PhIL1 followed by mass spectrometry. Immunoprecipitation and mass spectrometry (co-IP/MS) PLoS pathogens Low 28985225
2021 PIC2 (PF3D7_0822900) was enriched in a BioID proximity-labeling proteomics screen using PhIL1 as bait in asexual blood-stage P. falciparum parasites, consistent with its membership in the IMC-associated PhIL1 complex. BioID proximity-dependent biotin identification followed by mass spectrometry Cellular microbiology Low 33830607

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