Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis

Halina Offner, Bozena Celnik, Timothy S. Bringman, Denise Casentini-Borocz, Glenn E. Nedwin, Arthur A. Vandenbark

Research output: Contribution to journalArticle

179 Scopus citations

Abstract

Human placental tissue contains regulatory molecules that may prevent allo-sensitization. Recently, a 14 kDa β-galactoside binding protein with demonstrated immunoregulatory properties has been cloned using cDNA from human placenta and expressed in Escherichia coli. The present study assesses the ability of this recombinant immunomodulatory lectin (rIML-1), to prevent experimental autoimmune encephalomyelitis (EAE), a paralytic T cell-mediated disease directed against myelin basic protein (BP). Injection or rIML-1 into Lewis rats inhibited the induction of both clinical and histological signs of EAE, apparently by blocking sensitization of encephalitogenic BP-specific T cells and inducing BP-dependent suppressor cells. Because it is neither immunogenic nor toxic, rIML-1 may have application in humans, and would have distinct advantages over unselective cytotoxic immunosuppressive agents used currently in the treatment of autoimmune diseases and transplantation.

Original languageEnglish (US)
Pages (from-to)177-184
Number of pages8
JournalJournal of Neuroimmunology
Volume28
Issue number2
DOIs
StatePublished - Jul 1990

Keywords

  • Delayed-type hypersensitivity
  • Experimental autoimmune encephalomyelitis
  • Immunosuppression
  • Myelin basic protein
  • Recombinant β-galactoside binding human immunolectin
  • T cell line

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Neurology
  • Clinical Neurology

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