Guillain Barré syndrome (GBS): new insights in the molecular mimicry between C. jejuni and human peripheral nerve (HPN) proteins

J Neuroimmunol. 2015 Dec 15:289:168-76. doi: 10.1016/j.jneuroim.2015.11.005. Epub 2015 Nov 10.

Abstract

Profile and immunoreactivity of proteins from HPN tissue, and from Campylobacter jejuni (O:19) were investigated. Proteins were extracted, separated by SDS-PAGE, their cross reactivity monitored by Western blotting, and identified by nHPLC-nESI-HRMS analysis. Proteins from C. jejuni, at Mw ~70 KDa were chaperone/co-chaperone proteins (GroEL, DnaK and HtpG). In the corresponding HPN band were serum albumin, neurofilament light peptide, cytoskeletal keratins and one HSP 70 and one HSP60. These chaperones reciprocally share high primary sequence homology and conservation of their known epitopes. These findings suggest that HSP chaperones may be suitable candidates involved in the molecular mimicry triggering GBS.

Keywords: Campylobacter jejuni; Guillain–Barré syndrome; HPLC-HR-MS/MS; Heat shock proteins; Proteomics.

MeSH terms

  • Campylobacter jejuni / immunology
  • Campylobacter jejuni / metabolism*
  • Chromatography, High Pressure Liquid
  • Cross Reactions
  • Epitopes
  • Guillain-Barre Syndrome* / complications
  • Guillain-Barre Syndrome* / metabolism
  • Guillain-Barre Syndrome* / pathology
  • Humans
  • Keratins / metabolism*
  • Molecular Chaperones / metabolism*
  • Molecular Mimicry*
  • Molecular Weight
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Peripheral Nerves / metabolism*
  • Sequence Alignment
  • Spectrometry, Mass, Electrospray Ionization
  • Tandem Mass Spectrometry

Substances

  • Epitopes
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • Keratins