Proteomics

Dataset Information

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Novel antibody-peptide binding assay indicates presence of immunoglobulins against EGFR phospho-site S1166 in high-grade glioma.


ABSTRACT: The project’s aim was to develop and test the applicability of a method to determine the presence of serum immunoglobulins against specific autoantibodies. The method combined immunoglobulin G enrichment (using Melon Gel), molecular weight filtration, and targeted mass spectrometry and the feasibility was successfully tested in an experiment using a peptide library (tryptic digest) of dinitrophenyl labelled peptides and anti-DNP. In a second step, a phospho-peptide library, derived from glioblastoma multiform tissue, was tested against plasma samples from glioma patients and healthy donors, to determine the presence of complexes of IgG with immunoaffinity to EGFR or GFAP phospho-peptides. As a result, we found immunoaffinity to EGFR phospho-peptide GSHQIS[+80]LDNPDYQQDFFPK (covering the phospho-site S1166) in plasma of glioma patients.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human) Bos Taurus (bovine)

TISSUE(S): Glial Cell, Brain, Blood Plasma

DISEASE(S): Brain Glioma

SUBMITTER: Christoph Stingl  

LAB HEAD: Theo M. Luider

PROVIDER: PXD032844 | Pride | 2022-06-09

REPOSITORIES: Pride

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Publications

Novel Antibody-Peptide Binding Assay Indicates Presence of Immunoglobulins against EGFR Phospho-Site S1166 in High-Grade Glioma.

Zeneyedpour Lona L   Stingl Christoph C   Kros Johan M JM   Sillevis Smitt Peter A E PAE   Luider Theo M TM  

International journal of molecular sciences 20220502 9


We investigated the feasibility of detecting the presence of specific autoantibodies against potential tumor-associated peptide antigens by enriching these antibody-peptide complexes using Melon Gel resin and mass spectrometry. Our goal was to find tumor-associated phospho-sites that trigger immunoreactions and raise autoantibodies that are detectable in plasma of glioma patients. Such immunoglobulins can potentially be used as targets in immunotherapy. To that aim, we describe a method to detec  ...[more]

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