Microbial epitopes act as altered peptide ligands to prevent experimental autoimmune encephalomyelitis.
Microbial epitopes act as altered peptide ligands to prevent experimental autoimmune encephalomyelitis.
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DOI:
10.1084/jem.189.8.1275
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发表时间:
1999-04-19
期刊:
影响因子:
--
通讯作者:
Steinman L
中科院分区:
文献类型:
--
作者:
Ruiz PJ;Garren H;Hirschberg DL;Langer-Gould AM;Levite M;Karpuj MV;Southwood S;Sette A;Conlon P;Steinman L
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.