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 ID442526
Chemical TypeLinear peptide
Linear SequenceAPKSQIVML
Source Molecule NamePolyribonucleotide nucleotidyltransferase 1, mitochondrial
Source OrganismHomo sapiens (human)
Starting Position221
Ending Position229
Epitope Reference Details
Epitope Structure DefinesExact Epitope
Epitope NameEluted Peptide 306
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 SequenceAPKSQIVML
Source Molecule NamePolyribonucleotide nucleotidyltransferase 1, mitochondrial
Source OrganismHomo sapiens (human)
Starting Position221
Ending Position229
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