Immunoproteomics becomes a potent methodology used for classifying immunoreactive proteins. In this study, an immunoproteomic method based on 2-dimensional gel electrophoresis (2D-PAGE) and immunoblotting mutual with high-resolution mass spectrometry (MS)  used to classify immunoreactive proteins that might be involved in mechanisms of Guillain-Barré syndrome (GBS) development, regardless of their possible reciprocal molecular mimicry. Proteins isolated from C. jejune and human peripheral nerve tissue (HPN) were separated with 2D SDS-PAGE and subjected to western blotting using serum samples from GBS patients. The peptides generated after proteolysis of the immunoreactive proteins acquiesced to nanoflow-high performance liquid chromatography-nano electrospray ionization coupled to high-resolution mass spectrometry (HPLC-I-MS and MS/MS) followed by Sequestrated analysis for proteins identification. In  immunoreactivity was found for GroEL and DnaK, structural proteins (MOMP), key enzymatic proteins necessary for the microbial proliferation (adenylate kinase, enolase, inorganic pyrophosphatase and aspartate ammonia-lyase), and antioxidant enzymes (alkyl hydroperoxide reductase–AhpC and DNA protection during starvation protein - DNA protection factor against Fe2+-mediated oxidative stress).

  • Track 1-1 Comparative immunoproteomics
  • Track 2-2 MHC binding motifs
  • Track 3-3 immunoblotting
  • Track 4-4 2-D gel electrophoresis

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