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Microbial epitopes act as altered peptide ligands to prevent experimental autoimmune encephalomyelitis JOURNAL OF EXPERIMENTAL MEDICINE Ruiz, P. J., Garren, H., Hirschberg, D. L., Langer-Gould, A. M., Levite, M., Karpuj, M. V., Southwood, S., Sette, A., Conlon, P., Steinman, L. 1999; 189 (8): 1275-1283

Abstract

Molecular mimicry refers to structural homologies between a self-protein and a microbial protein. A major epitope of myelin basic protein (MBP), p87-99 (VHFFKNIVTPRTP), induces experimental autoimmune encephalomyelitis (EAE). VHFFK contains the major residues for binding of this self-molecule to T cell receptor (TCR) and to the major histocompatibility complex. Peptides from papilloma virus strains containing the motif VHFFK induce EAE. A peptide from human papilloma virus type 40 (HPV 40) containing VHFFR, and one from HPV 32 containing VHFFH, prevented EAE. A sequence from Bacillus subtilis (RKVVTDFFKNIPQRI) also prevented EAE. T cell lines, producing IL-4 and specific for these microbial peptides, suppressed EAE. Thus, microbial peptides, differing from the core motif of the self-antigen, MBPp87-99, function as altered peptide ligands, and behave as TCR antagonists, in the modulation of autoimmune disease.

View details for Web of Science ID 000079898600010

View details for PubMedID 10209044