BDP3

BDP3 (PF3D7_0110500) is a putative bromodomain-containing epigenetic reader protein in Plasmodium falciparum, identified through histone peptide pull-down proteomics as a member of the set of PTM-reader proteins associated with acetylated histone marks (PMID:31728527). Beyond this candidate reader assignment, BDP3 has been detected only as a component of a nuclear chromatin-modulation network: it co-purifies with PfMORC alongside HDAC1, SET3, PHD2, ISWI, and multiple ApiAP2 transcription factors (PMID:39636094), and appears in the proximity interactome of PfSET10 (PMID:39445823). All three observations are proteomic detections; no direct enzymatic activity, substrate or histone-mark specificity, structure, subcellular localization, or loss-of-function phenotype has been experimentally established for BDP3 itself in the available corpus. The current evidence therefore places BDP3 within a blood-stage chromatin-modulation network by association only, and does not define its individual molecular role.

1. 2019 Low

   To ask whether BDP3 acts as a chromatin reader, histone peptide affinity proteomics tested which parasite proteins bind modified histone tails, and placed BDP3 among candidate acetyl-histone readers.

   Evidence Quantitative histone peptide pull-down with mass spectrometry in P. falciparum

   PMID:31728527

   Open questions at the time

   • Single pull-down hit not individually validated; direct binding of BDP3 to a defined histone mark not confirmed
   • No specific acetyl-lysine mark or affinity measured for BDP3
   • No demonstration that the bromodomain of BDP3 mediates the interaction
2. 2024 Low

   To position BDP3 in a functional chromatin context, IP-MS of tagged PfMORC asked which proteins co-assemble with it, recovering BDP3 within a network including HDAC1, SET3, PHD2, ISWI, and ApiAP2 factors.

   Evidence Immunoprecipitation-mass spectrometry using PfMORC-HA tagged P. falciparum parasites

   PMID:39636094

   Open questions at the time

   • Single Co-IP without reciprocal pull-down from BDP3; direct vs indirect association undetermined
   • No functional experiment performed on BDP3 within the network
   • Stoichiometry and whether BDP3 is a stable versus transient component are unknown
3. 2024 Low

   Proximity labelling of PfSET10 tested BDP3's spatial proximity to another chromatin regulator, independently supporting its membership in a blood-stage nuclear chromatin-modulation network.

   Evidence TurboID proximity-labelling coupled with mass spectrometry in blood-stage P. falciparum

   PMID:39445823

   Open questions at the time

   • Proximity labelling indicates neighborhood, not direct interaction
   • No validation of BDP3-PfSET10 association by orthogonal method
   • No functional consequence of the association tested for BDP3

• The direct molecular function of BDP3 remains undefined: whether its bromodomain binds a specific acetylated histone mark, its subcellular localization, and its loss-of-function phenotype are all unestablished.
• No histone-mark binding specificity or affinity determined for BDP3
• No knockout/knockdown phenotype or essentiality data for BDP3
• No structural model or localization data specific to BDP3