Intact Transition Epitope Mapping - Targeted High-Energy Rupture of Extracted Epitopes (ITEM-THREE).
Affinity proteomics
Antibodies*
Assay development
BLAST
Immunology*
Ligand -Receptor Interactions*
Mass Spectrometry
Non-covalent interaction MS*
Protein complex analysis
Targeted mass spectrometry
Therapeutic antibodies*
data base search
epitope mapping
peptide sequencing
Journal
Molecular & cellular proteomics : MCP
ISSN: 1535-9484
Titre abrégé: Mol Cell Proteomics
Pays: United States
ID NLM: 101125647
Informations de publication
Date de publication:
08 2019
08 2019
Historique:
received:
04
03
2019
revised:
14
05
2019
pubmed:
31
5
2019
medline:
6
6
2020
entrez:
1
6
2019
Statut:
ppublish
Résumé
Epitope mapping, which is the identification of antigenic determinants, is essential for the design of novel antibody-based therapeutics and diagnostic tools. ITEM-THREE is a mass spectrometry-based epitope mapping method that can identify epitopes on antigens upon generating an immune complex in electrospray-compatible solutions by adding an antibody of interest to a mixture of peptides from which at least one holds the antibody's epitope. This mixture is nano-electrosprayed without purification. Identification of the epitope peptide is performed within a mass spectrometer that provides an ion mobility cell sandwiched in-between two collision cells and where this ion manipulation setup is flanked by a quadrupole mass analyzer on one side and a time-of-flight mass analyzer on the other side. In a stepwise fashion, immune-complex ions are separated from unbound peptide ions and dissociated to release epitope peptide ions. Immune complex-released peptide ions are separated from antibody ions and fragmented by collision induced dissociation. Epitope-containing peptide fragment ions are recorded, and mass lists are submitted to unsupervised data base search thereby retrieving both, the amino acid sequence of the epitope peptide and the originating antigen. ITEM-THREE was developed with antiTRIM21 and antiRA33 antibodies for which the epitopes were known, subjecting them to mixtures of synthetic peptides of which one contained the respective epitope. ITEM-THREE was then successfully tested with an enzymatic digest of His-tagged recombinant human β-actin and an antiHis-tag antibody, as well as with an enzymatic digest of recombinant human TNFα and an antiTNFα antibody whose epitope was previously unknown.
Identifiants
pubmed: 31147491
pii: S1535-9476(20)34057-3
doi: 10.1074/mcp.RA119.001429
pmc: PMC6683010
pii:
doi:
Substances chimiques
Actins
0
Antibodies
0
Antigen-Antibody Complex
0
Epitopes
0
Peptides
0
Ribonucleoproteins
0
SS-A antigen
0
TNF protein, human
0
Tumor Necrosis Factor-alpha
0
Banques de données
PDB
['1tnf.pdb']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1543-1555Informations de copyright
© 2019 Danquah et al.
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