Affinage · Plasmodium

PF3D7_1414100

zinc finger protein, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1414100 is a putative C2H2 zinc finger protein required for female sexual-stage development in Plasmodium; in a global barcoded-mutant screen it was identified as a female-determining factor essential for female gametocyte formation, and its protein interactors place it within germ-granule-like ribonucleoprotein complexes that complement transcriptional programs governing female development (PMID:36634679). Its P. falciparum ortholog can rescue the lethal proliferation defect of Toxoplasma gondii depleted of the C2H2 zinc finger protein TgZNF2, indicating a conserved mRNA nuclear export function (PMID:27385072). Beyond these findings, the direct molecular mechanism of PF3D7_1414100 in Plasmodium — its RNA targets, the composition of the ribonucleoprotein complexes it joins, and its subcellular site of action — has not been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2016 Low

    Whether the zinc-finger mRNA nuclear export activity defined in Toxoplasma is conserved in Plasmodium was unknown; cross-species complementation established functional conservation of the P. falciparum homolog.

    Evidence Expression of the P. falciparum homolog in inducible TgZNF2-knockout T. gondii, scoring rescue of the growth defect

    PMID:27385072

    Open questions at the time
    • Complementation was performed in Toxoplasma, not directly in Plasmodium, so the native Plasmodium function was not tested
    • Identity of the rescuing gene as PF3D7_1414100 is inferred, not explicitly confirmed
    • No direct demonstration of mRNA export activity or RNA substrates for the Plasmodium protein
  2. 2023 Medium

    The biological role of PF3D7_1414100 in the parasite life cycle was undefined; a genome-scale screen established it as essential for female sexual-form development and placed it in germ-granule-like ribonucleoprotein complexes.

    Evidence Global barcoded-mutant screen with single-cell transcriptomics of mutants and protein interaction network analysis in P. berghei and P. falciparum

    PMID:36634679

    Open questions at the time
    • Gene identity as PF3D7_1414100 inferred from screen context, not explicitly stated in the abstract
    • The RNA cargo and composition of the ribonucleoprotein complexes are not defined
    • Mechanistic link between the germ-granule association and the proposed mRNA export function is not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • The direct molecular mechanism of PF3D7_1414100 in Plasmodium — its RNA targets, the subunits of its ribonucleoprotein complexes, its localization, and whether it directly mediates mRNA nuclear export in the parasite — remains unresolved.
  • No direct RNA substrates identified in Plasmodium
  • No structural or biochemical characterization of the zinc finger's activity
  • No native localization or reciprocal interaction validation reported

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
germ-granule-like ribonucleoprotein complex [#0]

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2023 In a global barcoded-mutant screen, PF3D7_1414100 (identified as a female-determining zinc-finger protein) was found to be essential for female sexual form development in Plasmodium; protein interactors of this zinc-finger protein indicate it participates in germ-granule-like ribonucleoprotein complexes, complementing transcriptional processes in the regulation of female development. Global screen of barcoded mutants; single-cell transcriptomics of mutant parasites; protein interaction network analysis Cell host & microbe Medium 36634679
2016 The P. falciparum homolog of Toxoplasma gondii TgZNF2 (a C2H2 zinc finger protein) was able to efficiently rescue the lethal proliferation defect caused by TgZNF2 depletion in T. gondii, suggesting that the mRNA nuclear export function of this zinc-finger protein is conserved in P. falciparum. Complementation assay: expression of P. falciparum homolog in inducible TgZNF2-knockout T. gondii parasites; phenotypic rescue of growth defect Cellular microbiology Low 27385072

Source papers

Stage 0 corpus · 8 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2023 Regulators of male and female sexual development are critical for the transmission of a malaria parasite. Cell host & microbe 53 36634679
2021 Zinc finger proteins of Plasmodium falciparum. Cellular microbiology 33 34418264
2022 The Plasmodium falciparum CCCH Zinc Finger Protein ZNF4 Plays an Important Role in Gametocyte Exflagellation through the Regulation of Male Enriched Transcripts. Cells 20 35626703
2016 An evolutionary conserved zinc finger protein is involved in Toxoplasma gondii mRNA nuclear export. Cellular microbiology 14 27385072
2016 Plasmodium falciparum Hep1 Is Required to Prevent the Self Aggregation of PfHsp70-3. PloS one 9 27253881
2023 The Plasmodium falciparum CCCH zinc finger protein MD3 regulates male gametocytogenesis through its interaction with RNA-binding proteins. Molecular microbiology 8 38148574
2017 Multifunctional Involvement of a C2H2 Zinc Finger Protein (PbZfp) in Malaria Transmission, Histone Modification, and Susceptibility to DNA Damage Response. mBio 5 28851851
2026 The CCCH-type zinc-finger Pf MD3 promotes translation for malaria parasite transmission. bioRxiv : the preprint server for biology 0 42244567