PXD074377

PXD074377 is an original dataset announced via ProteomeXchange.

Title	The N’ terminus of Alpha-1 Giardin, a parasitic annexin orthologue, is essential for oligomerization and lipid-binding activity
Description	We present a functional analysis of alpha-giardins (αGs), with a particular focus on α1-giardin (α1G), a leading vaccine candidate against giardiasis and a putative virulence-associated UPS substrate. We show that αGs localize to peripheral endocytic compartments (PECs), specialized endo-lysosomal organelles implicated in protein release, and engage in multiprotein complexes enriched in UPS substrates. Using lipid-binding assays, cross-linking mass spectrometry (XL-MS), and structural modelling, we define conserved and divergent features of αG membrane interactions. Focusing on α1G, we combine site-directed mutagenesis, confocal microscopy, and mass photometry to demonstrate a critical role for its short N-terminal region in oligomerization and membrane association. Integration of these data with molecular dynamics simulations reveals how α1G oligomeric state and membrane occupancy are regulated at PEC membranes. Together, our findings establish a mechanistic framework for annexin-mediated UPS in Giardia and provide structural insights relevant to parasite virulence and vaccine development.
HostingRepository	PRIDE
AnnounceDate	2026-06-11
AnnouncementXML	Submission_2026-06-11_01:40:31.318.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Manfred Heller
SpeciesList	scientific name: Giardia intestinalis assemblage A; NCBI TaxID: NEWT:941442;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2026-02-11 23:54:25	ID requested
⏵ 1	2026-06-11 01:40:31	announced

10.64898/2026.01.09.697555;

submitter keyword: lipid, molecular dynamics, annexin A5, unconventional secretion, PIP, oligomerization, endocytic compartments, membrane-binding, Giardia lamblia,Alpha-giardin

Carmen Faso
contact affiliation	Institute of Cell Biology, University of Bern
contact email	carmen.faso@unibe.ch
lab head
Manfred Heller
contact affiliation	Proteomics and Mass Spectrometry Core Facility, Departement for Biomedical Research, University of Berne
contact email	pmscf.dbmr@unibe.ch
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD074377
     1. Label: PRIDE project
     2. Name: The N’ terminus of Alpha-1 Giardin, a parasitic annexin orthologue, is essential for oligomerization and lipid-binding activity