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Related Experiment Videos

A T cell epitope for experimental allergic neuritis.

T Olee1, J M Powers, S W Brostoff

  • 1Department of Neurology, Medical University of South Carolina, Charleston 29425.

Journal of Neuroimmunology
|August 1, 1988
PubMed
Summary

A synthetic peptide from bovine P2 protein (residues 57-81) induced severe experimental allergic neuritis (EAN) in rats. A shorter peptide (60-81) also caused EAN, identifying a minimal T cell antigenic site.

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Area of Science:

  • Neuroimmunology
  • Protein Chemistry

Background:

  • Experimental allergic neuritis (EAN) is an animal model for Guillain-Barré syndrome.
  • The P2 protein is a key component of myelin in the peripheral nervous system and a known autoantigen in EAN.

Purpose of the Study:

  • To identify the specific peptide sequences of the bovine P2 protein responsible for inducing experimental allergic neuritis (EAN).
  • To investigate the minimal sequence required for T cell recognition and induction of EAN.

Main Methods:

  • Synthesis of bovine P2 protein peptides (residues 57-81 and 60-81).
  • Induction of EAN in Lewis rats using synthetic peptides.
  • Establishment and use of P2 protein-specific T cell lines for passive transfer experiments.

Main Results:

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  • The synthetic peptide representing residues 57-81 of the bovine P2 protein induced severe paralytic EAN in Lewis rats.
  • A smaller peptide, residues 60-81, also induced EAN, albeit a milder form, representing the shortest sequence found to date that can elicit clinical EAN.
  • P2 protein-specific T cell lines could transfer paralytic EAN to naive rats, confirming the role of T cells in the disease.

Conclusions:

  • Specific peptide sequences within the bovine P2 protein are critical for the induction of experimental allergic neuritis.
  • The minimal antigenic site for T cell recognition and EAN induction is located within residues 60-81 of the P2 protein.
  • Structural predictions suggest that amphipathic alpha-helical structures may represent T cell antigenic sites.