Affinage · Plasmodium

SYN13

PF3D7_1104100 · syntaxin, Qa-SNARE family

Audit flag: identity unverified
Annotated
2026-09-08
11 papers in source corpus 4 papers cited in narrative 4 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1104100 (SYN13) is a Qa-SNARE/syntaxin-family protein of Plasmodium falciparum known only from genome-wide bioinformatic surveys, which catalogued it among the SNARE-like proteins of the parasite and placed it within a P. falciparum-specific syntaxin-like subfamily (PMID:17240462); subsequent genome mining classified it as one of seven parasite Qa-SNAREs (PMID:19103232). No direct experiment in the available corpus has established the subcellular localization, binding partners, enzymatic activity, or cellular function of SYN13 itself: in each survey, direct localization was reported only for other family members (PfSyn5p, PfSec22p, PfStx1), not SYN13 (PMID:17240462, PMID:19103232). Broader functional studies of the P. falciparum SNARE complement characterized Stx12 and Stx16/Stx6 in trafficking and inner membrane complex biogenesis, but did not experimentally interrogate SYN13 (PMID:33082261). Beyond its membership in the syntaxin/Qa-SNARE family, no mechanistic detail specific to PF3D7_1104100 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 4 steps
  1. 2006 Low

    Establishing the parasite's SNARE repertoire was the first step toward understanding its membrane trafficking; this survey placed SYN13 on the map as a syntaxin-like protein within a P. falciparum-specific subfamily.

    Evidence Bioinformatic and phylogenetic analysis of the P. falciparum genome, with GFP-tagging of select (non-SYN13) family members

    PMID:17240462

    Open questions at the time
    • Identification is computational only; no direct experiment was performed on SYN13/PF3D7_1104100
    • Subcellular localization of SYN13 was not reported
    • No binding partners or function assigned
  2. 2008 Low

    Refining the Qa-SNARE subset and predicting intracellular locations aimed to assign each syntaxin to a trafficking step, but SYN13's predicted location was never experimentally tested.

    Evidence Genome mining, sequence alignment, and gene-structure confirmation; direct localization confirmed only for PfStx1

    PMID:19103232

    Open questions at the time
    • SYN13 localization was predicted computationally, not validated
    • No cognate SNARE partners identified for SYN13
    • No functional or knockdown data for SYN13
  3. 2020 Low

    Functional dissection of individual parasite SNAREs began to link specific syntaxins to defined trafficking routes, yet SYN13 remained only a listed member of the assessed complement rather than an experimental subject.

    Evidence Conditional knockdown, co-immunoprecipitation with SEC1/Munc18 tethering factors, and fluorescence microscopy of Stx12 and Stx16/Stx6 (not SYN13)

    PMID:33082261

    Open questions at the time
    • No experiment in the study addresses SYN13/PF3D7_1104100 directly
    • SYN13 trafficking role, partners, and essentiality remain untested
  4. 2026 Low

    A syntaxin-5-like parasite protein ('PfSyn5') was characterized as a mosquito midgut-factor binding partner and transmission-blocking antibody target, but the abstract does not map 'PfSyn5' to PF3D7_1104100, so this cannot be attributed to SYN13.

    Evidence Biochemical interaction pulldown/binding assays plus infection assays with recombinant protein and blocking antibodies (preprint)

    PMID:42146686

    Open questions at the time
    • Gene identity of 'PfSyn5' relative to PF3D7_1104100 is not confirmed; attribution to SYN13 is uncertain
    • Single-lab preprint not independently confirmed
    • No direct evidence that SYN13 mediates the reported interaction or transmission phenotype

Open questions

Synthesis pass · forward-looking unresolved questions
  • The core mechanistic questions for SYN13 remain entirely open: its subcellular localization, cognate SNARE and Munc18/SEC1 partners, the membrane-fusion step it catalyzes, and its role in parasite biology are all uncharacterized in the available corpus.
  • No experimental localization of SYN13
  • No identified binding partners or complex membership for SYN13 specifically
  • No knockdown/knockout phenotype defining its cellular function

Mechanism profile

Synthesis pass · controlled-vocabulary classification
No controlled-vocabulary terms were assigned to this entry.

Evidence

Reading pass · 4 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 PF3D7_1104100 (SYN13) was identified as one of 18 SNARE-like proteins in the P. falciparum genome via bioinformatics analysis; it was classified into a P. falciparum-specific syntaxin-like subfamily. The study determined subcellular localizations of select family members by GFP-tagging, but direct localization of SYN13 specifically was not reported. Bioinformatics/phylogenetic analysis of P. falciparum genome; GFP-tagging of select family members (PfSyn5p and PfSec22p, not SYN13 directly) Molecular and biochemical parasitology Low 17240462
2008 Seven Qa-SNAREs were identified in the P. falciparum genome including PF3D7_1104100 (SYN13); comprehensive sequence alignments were used to predict intracellular locations for all seven, but direct experimental localization was only confirmed for PfStx1 (not SYN13). Genome mining, sequence alignment, gene structure confirmation; direct localization experiment performed only on PfStx1 Molecular and biochemical parasitology Low 19103232
2020 In P. falciparum, the SNARE protein Stx12 (described as localizing to an endosomal-like compartment and involved in trafficking to rhoptries, micronemes, and apicoplast) and Stx16/Stx6 (implicated in inner membrane complex biogenesis) were functionally characterized; SYN13/PF3D7_1104100 was not directly studied but is listed as part of the broader P. falciparum SNARE complement assessed in this work. Conditional knockdown, co-immunoprecipitation with SEC1/Munc18 tethering factors, fluorescence microscopy mBio Low 33082261
2026 The P. falciparum syntaxin-5-like protein PfSyn5 (described in the abstract as the parasite binding partner of the Anopheles gambiae midgut factor AgMOBP1) was identified by biochemical interaction assays. Anti-PfSyn5 polyclonal antibodies blocked malaria transmission with complete inhibition at 1 μg/mL and an estimated IC50 of ~3 ng/mL (~20 pM). Note: the abstract uses the name 'PfSyn5' for this interaction partner; based on context this may correspond to a syntaxin family member but the abstract does not explicitly map 'PfSyn5' to PF3D7_1104100. Attribution to SYN13/PF3D7_1104100 is uncertain. Biochemical interaction assays (pulldown/binding), functional infection assay with recombinant protein and blocking antibodies bioRxiv : the preprint server for biologypreprint Low 42146686

Source papers

Stage 0 corpus · 11 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Identification of Plasmodium falciparum family of SNAREs. Molecular and biochemical parasitology 38 17240462
2020 The ZIP Code of Vesicle Trafficking in Apicomplexa: SEC1/Munc18 and SNARE Proteins. mBio 33 33082261
2019 Plasmodium Secretion Induces Hepatocyte Lysosome Exocytosis and Promotes Parasite Entry. iScience 21 31731198
2012 The isoprenoid-precursor dependence of Plasmodium spp. Natural product reports 19 22555616
2010 Evidence for prenylation-dependent targeting of a Ykt6 SNARE in Plasmodium falciparum. Molecular and biochemical parasitology 19 21075148
2014 Computational prediction of protein interactions related to the invasion of erythrocytes by malarial parasites. BMC bioinformatics 14 25433733
2009 The longin domain regulates the steady-state dynamics of Sec22 in Plasmodium falciparum. Eukaryotic cell 7 19617396
2008 Plasmodium falciparum secretory pathway: characterization of PfStx1, a plasma membrane Qa-SNARE. Molecular and biochemical parasitology 7 19103232
2026 Host SNARE Proteins Mediate Lysosome and PVM Fusion to Support Plasmodium Liver Infection. Cells 1 41972675
2026 Disruption of the AgMOBP1-PfSyn5 interface abolishes malaria transmission. bioRxiv : the preprint server for biology 0 42146686
2026 VAMP3 vesicles support host protein recruitment and Plasmodium liver stage development. mBio 0 42478859