An Altered Peptide Ligand Mediates Immune Deviation and Prevents Autoimmune Encephalomyelitis

Nicholson, LB, Greer, JM, Sobel, RA, Lees, MB and Kuchroo, VK (1995) An Altered Peptide Ligand Mediates Immune Deviation and Prevents Autoimmune Encephalomyelitis. Immunity, 3 4: 397-405. doi:10.1016/1074-7613(95)90169-8


Author Nicholson, LB
Greer, JM
Sobel, RA
Lees, MB
Kuchroo, VK
Title An Altered Peptide Ligand Mediates Immune Deviation and Prevents Autoimmune Encephalomyelitis
Journal name Immunity   Check publisher's open access policy
ISSN 1074-7613
Publication date 1995-10-01
Year available 1995
Sub-type Article (original research)
DOI 10.1016/1074-7613(95)90169-8
Open Access Status Not yet assessed
Volume 3
Issue 4
Start page 397
End page 405
Total pages 9
Place of publication CAMBRIDGE
Publisher CELL PRESS
Language eng
Abstract In experimental autoimmune encephalomyelitis (EAE) induced with myelin proteolipid protein (PLP) peptide 139-151, we have previously shown that the disease is mediated by Th1 cells, which recognize tryptophan 144 as the primary TCR contact point. Here we describe an altered peptide ligand (APL), generated by a single amino acid substitution (tryptophan to glutamine) at position 144 (Q144), which inhibits the development of EAE induced with the native PLP 139-151 peptide (W144). We show that the APL induces T cells that are cross-reactive with the native peptide and that these cells produce Th2 (IL-4 and IL-10) and Th0 (IFN gamma and IL-10) cytokines. Adoptive transfer of T cell lines generated with the APL confer protection from EAE. These data show that changing a single amino acid in an antigenic peptide can significantly influence T cell differentiation and suggest that immune deviation may be one of the mechanisms by which APLs can inhibit an autoimmune disease.
Keyword T-Cell Receptor
Experimental Allergic Encephalomyelitis
Myelin Proteolipid Protein
Basic-Protein
Mice
Expression
Inhibition
Secretion
Cytokines
Interleukin-4
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID NS 16945
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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