Affinage · Toxoplasma gondii

AAP5

apical annuli protein AAP5 · UniProt S8F9P9

Annotated
2026-09-10
1 papers in source corpus 1 papers cited in narrative 3 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AAP5 is a component of the apical annuli of Toxoplasma gondii, a set of structures embedded within the inner membrane complex (IMC) sutures, where it was identified and validated by reciprocal proximity biotinylation (BioID) proteomics and super-resolution microscopy as one of five apical annuli proteins (AAP1–5) (PMID:31470470). Within this structure, AAP5 forms part of a concentric, pore-like ring assembly of 200–400 nm diameter built from coiled-coil and signalling domain-containing proteins together with Centrin2 (PMID:31470470). No direct functional mechanism for AAP5 itself has been experimentally defined in the available corpus; its narrow conservation among internally budding coccidians is the only basis for an inferred role.

Mechanistic history

Synthesis pass · year-by-year structured walk · 3 steps
  1. 2019 Medium

    Establishing what proteins constitute the apical annuli answered where AAP5 resides in the parasite, placing it as a bona fide structural component of the IMC sutures rather than a diffuse cytoplasmic factor.

    Evidence Reciprocal BioID proteomics with super-resolution microscopy validation in Toxoplasma gondii

    PMID:31470470

    Open questions at the time
    • No functional rescue or mutagenesis of AAP5 specifically
    • Molecular activity of AAP5 within the complex not defined
  2. 2019 Medium

    Resolving the architecture of the apical annuli showed AAP5 sits within a concentric pore-like ring, defining the structural context in which it operates alongside Centrin2 and coiled-coil/signalling proteins.

    Evidence Super-resolution microscopy, BioID, and domain analysis in Toxoplasma gondii

    PMID:31470470

    Open questions at the time
    • AAP5's specific contribution to ring assembly or integrity untested
    • Function of the pore-like structure unknown
  3. 2019 Low

    Phylogenetic restriction of AAP5 to internally budding coccidians offered a first hypothesis linking the protein to replication by internal budding, though without direct functional testing.

    Evidence Phylogenetic analysis

    PMID:31470470

    Open questions at the time
    • Computational inference only, no functional experiment
    • Connection to internal budding untested experimentally

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Apical annuli complex (AAP1–5 with Centrin2)

Evidence

Reading pass · 3 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2019 AAP5 was identified as a component of the apical annuli structures in Toxoplasma gondii by reciprocal proximity biotinylation (BioID) proteomics and validated as one of five apical annuli proteins (AAP1–5) residing within the inner membrane complex (IMC) sutures. Reciprocal proximity biotinylation (BioID) proteomics; super-resolution microscopy Cellular microbiology Medium 31470470
2019 The apical annuli complex, which includes AAP5, is organized as a concentric pore-like structure with four rings of 200–400 nm diameter, embedded in the IMC sutures, and is composed of coiled-coil and signalling domain-containing proteins together with Centrin2. Super-resolution microscopy; BioID proteomics; domain analysis Cellular microbiology Medium 31470470
2019 Phylogenetic analysis showed that AAP5 is conserved narrowly within coccidian apicomplexans that multiply by internal budding, suggesting a functional role linked to internal budding replication. Phylogenetic analysis Cellular microbiology Low 31470470

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2019 The apical annuli of Toxoplasma gondii are composed of coiled-coil and signalling proteins embedded in the inner membrane complex sutures. Cellular microbiology 38 31470470