Biological activity of recombinant human myelin basic protein

Henry F. Oettinger, Ahmad Al-Sabbagh, Zhang Jingwu, Janine M LaSalle, Howard L. Weiner, David A. Hafler

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Using an inducible expression vector in Escherichia coli, we have expressed, purified, and biologically characterized recombinant human myelin basic protein (r-MBP). The recombinant protein binds in cation-exchange chromatography with similar affinity to purified, human MBP, and elutes as single, 18.5-kDa species as judged by SDS-PAGE. The recombinant protein exhibits similar conformation to native MBP, as demonstrated by ELISA reactivity with a panel of six monoclonal antibodies directed against at least three different epitopes on human MBP. Additionally, recombinant MBP can trigger the proliferation of human T cell clones recognizing MBP, can induce experimental autoimmune encephalomyelitis (EAE) in the SJL mouse, and is capable of suppressing EAE following tolerization via oral administration. Most important, by using a novel method of purification, the recombinant protein preparation contains no detectable proteolytically derived fragments of MBP, a significant advantage over MBP purifed from protease-rich central nervous system tissue. Purified recombinant MBP produced in e. coli will be useful as a biological reagent where highly purified protein devoid of degradation products is needed. Relevance to the study of antigen processing, interactions between MHC and the TCR, as well as for investigation of antigen-driven immune tolerance are discussed.

Original languageEnglish (US)
Pages (from-to)157-162
Number of pages6
JournalJournal of Neuroimmunology
Issue number2
StatePublished - 1993
Externally publishedYes


  • Autoimmunity
  • Myelin
  • Myelin basic protein
  • Purification
  • Recombinant protein
  • T cell

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy
  • Clinical Neurology
  • Neurology


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