Affinage · Plasmodium

ALP2b

PF3D7_0505200 · actin-like protein, putative

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

ALP2b (PF3D7_0505200) is a putative actin-like protein whose only characterized role in the available corpus is as a co-purifying component of chromatin remodeling complexes. In P. falciparum, ALP2b was detected as part of the PfSWR1 complex through affinity pulldown of the shared NuA4/SWR1 subunit PfEAF2 followed by mass spectrometry (PMID:38564734). In P. berghei, its ortholog (PBANKA_1104800) co-immunoprecipitated with PbARID, a subunit of a SWI/SNF chromatin remodeling complex, placing it among the actin-related proteins that may associate with the ATPase subunit gSNF2 via an HSA domain (PMID:38554111). Beyond this complex membership, no direct functional characterization of ALP2b — its biochemical activity, direct binding partners, or a specific role separable from the complex — has been reported in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2024 Low

    Establishing the physical context of ALP2b addressed whether this putative actin-like protein associates with nuclear chromatin machinery, by placing it within the PfSWR1 remodeling complex.

    Evidence Affinity pulldown with PfEAF2 bait followed by mass spectrometry in P. falciparum

    PMID:38564734

    Open questions at the time
    • Single pulldown/MS identification with no reciprocal pulldown, mutagenesis, or functional validation specific to ALP2b
    • Direct binding partner within the complex not established
    • Whether ALP2b has a role separable from the complex is unknown
  2. 2024 Low

    The orthologous finding tested whether ALP2b's complex association is conserved, showing the P. berghei ortholog co-purifies with a SWI/SNF subunit and may contact the gSNF2 ATPase.

    Evidence Co-immunoprecipitation with PbARID bait followed by mass spectrometry (RIME) in P. berghei

    PMID:38554111

    Open questions at the time
    • Single co-IP/MS identification with no direct binding assay for ALP2b with gSNF2
    • HSA-domain-mediated interaction inferred, not demonstrated for this protein
    • No functional or phenotypic assay of ALP2b loss

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether ALP2b performs any specific molecular function within these remodeling complexes — and whether it is essential, structural, or regulatory — remains unresolved.
  • No direct binding assay confirming interaction with gSNF2 or other subunits
  • No genetic knockout/knockdown phenotype for ALP2b
  • No biochemical demonstration of actin-like activity

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
PfSWR1 chromatin remodeling complex (P. falciparum)SWI/SNF chromatin remodeling complex (P. berghei)

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2024 ALP2b (PF3D7_0505200) was identified as a component of the PfSWR1 chromatin remodeling complex in P. falciparum, detected by pulldown of PfEAF2 (a shared subunit of NuA4 and SWR1 complexes) followed by mass spectrometry. Affinity pulldown (PfEAF2 bait) followed by mass spectrometry identification mSphere Low 38564734
2024 The P. berghei ortholog of ALP2b (PBANKA_1104800) was identified as a co-immunoprecipitated protein with PbARID, a subunit of a SWI/SNF chromatin remodeling complex, suggesting ALP2b may interact with the ATPase subunit gSNF2 via its HSA domain as one of the actin-related proteins associated with the SWI/SNF complex. Co-immunoprecipitation (PbARID bait) followed by mass spectrometry (RIME) Nucleic acids research Low 38554111

Source papers

Stage 0 corpus · 3 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2026 Plasmodium Actin-Like Proteins 3 and 5a Are Required for Subsequent Steps of Mosquito Infection. Molecular microbiology 0 42629988
2024 PbARID-associated chromatin remodeling events are essential for gametocyte development in Plasmodium. Nucleic acids research 0 38554111
2024 MYST regulates DNA repair and forms a NuA4-like complex in the malaria parasite Plasmodium falciparum. mSphere 0 38564734