Abstract
EXPERIMENTAL allergic encephalomyelitis (EAE) is an autoimmune demyelinating disease induced by sensitisation to whole central nervous system (CNS) tissue homogenates, to myelin basic protein (BP) or to peptide regions derived from BP1–4. One such region, peptide E, was isolated from the pepsin digest of the BP and induces EAE in guinea pigs3,5. The shortest segment of peptide E which induces EAE, H-Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys-OH (peptide S3), has been synthesised by the Merrifield procedure6. Studies with analogous synthetic peptides with single amino acid residue substitutions have shown that the linearly spaced array of tryptophan, glutamine and lysine is needed to induce EAE6. We have now determined the minimum snbstitution in the amino acid sequence of peptide S3 necessary to destroy encephalitogenicity and to preserve the sequence for delayed hypersensitivity (DTH), also reported for peptide S37. The sequence requirement for induction of EAE is not restricted to tryptophan, glutamine and lysine, and certain analogous peptides retain the ability to induce and elicit DTH unaccompanied by signs of EAE.
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HASHIM, G., SHARPE, R. Non-encephalitogenic synthetic analogues of the determinant for allergic encephalomyelitis in guinea pigs. Nature 255, 484–485 (1975). https://doi.org/10.1038/255484a0
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DOI: https://doi.org/10.1038/255484a0
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