Reference
Reference TypeLiterature
TitleHLA-B and cysteinylated ligands distinguish the antigen presentation landscape of extracellular vesicles.
AuthorsJulia Bauzá-Martinez; Albert J R Heck; Wei Wu
AffiliationsBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomics Centre, Utrecht, The Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands. w.wu1@uu.nl; Netherlands Proteomics Centre, Utrecht, The Netherlands. w.wu1@uu.nl.
JournalCommun Biol
Year2021
AbstractExtracellular vesicles can modulate diverse processes ranging from proliferation and tissue repair, to chemo-resistance and cellular differentiation. With the advent of tissue and immunological targeting, extracellular vesicles are also increasingly viewed as promising vectors to deliver peptide-based cancer antigens to the human immune system. Despite the clinical relevance and therapeutic potential of such 'cell-free' approaches, the natural antigen presentation landscape exported in extracellular vesicles is still largely uncharted, due to the challenging nature of such preparations and analyses. In the context of therapeutic vesicle production, a critical evaluation of the similarity in vesicular antigen presentation is also urgently needed. In this work, we compared the HLA-I peptide ligandomes of extracellular vesicles against that of whole-cells of the same cell line. We found that extracellular vesicles not only over-represent HLA-B complexes and peptide ligands, but also cysteinylated peptides that may modulate immune responses. Collectively, these findings describe the pre-existing provision of vesicular HLA complexes that may be utilized to carry peptide vaccines, as well as the propensity for different peptide and post-translationally modified ligands to be presented, and will outline critical considerations in devising novel EV vaccination strategies.
Curation Last Updated2025-02-11 02:37:31
Epitope
Epitope ID418990
Chemical TypeLinear peptide
Linear SequenceIPAEGRVAL
Source Molecule NameGlyoxylate reductase/hydroxypyruvate reductase
Source OrganismHomo sapiens (human)
Starting Position15
Ending Position23
Epitope Reference Details
Epitope Structure DefinesExact Epitope
Epitope NameEluted Peptide 771
Location of Data in ReferenceFigure 2E-F
In Vivo Processing
Host OrganismHomo sapiens (human)
Host Details
SexM
MHC Types presentHLA-A*02:01;HLA-B*07:02;HLA-C*07:02
In Vivo Process
In Vivo Process TypeNo immunization
Disease Statehealthy
Antigen Processing Comments
Antigen Processing CommentsExtracellular vesicles and whole-cell lysates were collected from JY cells and subjected to MHC ligand elution using the pan-Class I Ab W6/32.
MHC Ligand Assay
Qualitative MeasurementPositive
Method/Techniquecellular MHC/mass spectrometry
Measurement ofligand presentation
Antigen Presenting Cells
Cell Tissue TypeBlood
Cell TypeJY cells-B cellhttp://purl.obolibrary.org/obo/CLO_0037202
Cell Culture ConditionsCell Line / Clone (EBV transformed, B-LCL)
MHC Allele
MHC Allele NameHLA-B*07:02
MHC Evidence CodeStatistically inferred by motif or alleles present
MHC Ligand
Epitope RelationEpitope
Chemical TypeLinear peptide
Linear SequenceIPAEGRVAL
Source Molecule NameGlyoxylate reductase/hydroxypyruvate reductase
Source OrganismHomo sapiens (human)
Starting Position15
Ending Position23
Assay Reference Details
Assay Comments by IEDB CuratorThe peptide was eluted from the following sources: Extracellular vesicles, Whole-cell lysates.
Location of Assay Data in ReferenceFigure 2E-F