Affinage · Plasmodium

PF3D7_1202300

dynein heavy chain, putative

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

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1202300 is annotated as a putative dynein heavy chain, and direct functional characterization of the P. falciparum protein itself is limited in the available corpus. The strongest mechanistic evidence derives from the P. yoelii ortholog DHC3, which localizes to subpellicular microtubules throughout ookinete morphogenesis and, when disrupted, impairs ookinete development, shape, gliding, and mosquito infection; DHC3-deficient ookinetes show defective formation or localization of apical organelles (PMID:39366980). In P. yoelii, Rab11A and Rab11B interact with DHC3 at subpellicular microtubules in a DHC3-dependent manner, identifying them as cargo receptors for this microtubule-associated dynein motor (PMID:39366980). In P. falciparum, a dynein heavy chain-like protein has been identified only as a target of oxidative adduction, forming 4-hydroxynonenal conjugates upon plakortin treatment (PMID:26459031). Beyond the P. yoelii ortholog data (PMID:39366980) and this oxidative-damage identification (PMID:26459031), no direct functional characterization of PF3D7_1202300 has been reported in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2015 Low

    The question of whether a dynein heavy chain-like protein participates in the response to peroxide antimalarials was addressed by identifying it as a target of oxidative adduction.

    Evidence Mass spectrometry identification of 4-HNE-protein conjugates in plakortin-treated P. falciparum

    PMID:26459031

    Open questions at the time
    • Gene-level validation that the adducted protein is PF3D7_1202300 specifically is absent
    • No functional consequence of the adduction was tested
    • No connection to the protein's normal cellular role was established
  2. 2024 Medium

    The cellular function of this dynein heavy chain was defined in the ortholog DHC3, establishing it as a subpellicular microtubule-associated motor required for ookinete morphogenesis and apical organelle organization.

    Evidence Genetic KO, fluorescence localization, co-immunoprecipitation, and ookinete/mosquito infection assays in P. yoelii

    PMID:39366980

    Open questions at the time
    • Correspondence between P. yoelii DHC3 and PF3D7_1202300 is inferred, not experimentally confirmed
    • Minus-end-directed motor activity and direct cargo transport were not reconstituted biochemically
    • No functional characterization was performed in P. falciparum itself

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether PF3D7_1202300 in P. falciparum performs the microtubule-associated dynein transport role established for the P. yoelii ortholog remains unresolved.
  • No direct genetic disruption or localization of PF3D7_1202300 in P. falciparum has been reported
  • Rab11A/B interaction has not been tested for the P. falciparum protein
  • The identity linking the ortholog studies to PF3D7_1202300 is unconfirmed

Mechanism profile

Synthesis pass · controlled-vocabulary classification

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2024 In P. yoelii ookinetes, DHC3 (a dynein heavy chain) localizes to subpellicular microtubules (SPMTs) throughout ookinete morphogenesis; its disruption impairs ookinete development, shape, and gliding, leading to failure in mosquito infection. DHC3-deficient ookinetes show defective formation or localization of apical organelles and structures. Rab11A and Rab11B interact with DHC3 at SPMTs in a DHC3-dependent manner, identifying them as receptors for cargoes driven by the SPMT-dynein motor. Genetic disruption (KO), fluorescence localization, co-immunoprecipitation/interaction assays, ookinete morphogenesis and gliding assays, mosquito infection assays Nature communications Medium 39366980
2015 In P. falciparum, the dynein heavy chain-like protein forms 4-hydroxynonenal (4-HNE) conjugates upon plakortin treatment, with specific binding sites identified by mass spectrometry, implicating it as a target of oxidative stress-mediated damage during peroxide-based antimalarial activity. Mass spectrometry identification of 4-HNE-protein conjugates Free radical biology & medicine Low 26459031

Source papers

Stage 0 corpus · 3 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 Oxidative stress-mediated antimalarial activity of plakortin, a natural endoperoxide from the tropical sponge Plakortis simplex. Free radical biology & medicine 27 26459031
2024 A subpellicular microtubule dynein transport machinery regulates ookinete morphogenesis for mosquito transmission of Plasmodium yoelii. Nature communications 5 39366980
2020 Definition of constitutive and stage-enriched promoters in the rodent malaria parasite, Plasmodium yoelii. Malaria journal 5 33228734