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,
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Multiple Sclerosis Research Laboratory, Department of Neurology, and
Department of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030; and
Neurology Research Laboratory, Veterans Affairs Medical Center, Houston, TX 77030
Th0 clones recognizing an immunodominant peptide of myelin basic
protein (residues 83–99) were derived from patients with multiple
sclerosis. We demonstrate that analogue peptides with alanine
substitution at Val86 and His88 had a unique
partial agonistic property in inducing Th0 
Th1 and Th0 Th2
deviation of the myelin basic protein-reactive T cell clones,
respectively. Th0 to Th1 deviation induced by peptide 86VA
correlated with up-regulation of Fyn and ZAP-70 kinase activities.
Conversely, Th0 to Th2 deviation induced by peptide 88HA was
associated with complete failure to activate Fyn and ZAP-70 kinases.
The observed Th1 and Th2 shift also correlated, to a lesser extent,
with Lck kinase activity that was down-regulated with Th1 deviation and
increased with Th2 deviation in some T cell clones. We demonstrated
that the Th1 and Th2 shift induced by the analogue peptides was a
reversible process, as the T cell clones previously exposed to either
86VA or 88HA peptide could revert to an opposite phenotype when
rechallenged reciprocally with a different analogue peptide. The study
has important implications in our understanding of regulation of
TCR-associated tyrosine kinases by altered peptide ligands and its role
in cytokine regulation of autoreactive T cells.
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