T cells discriminate between differentially phosphorylated forms of alpha B-crystallin, a major central nervous system myelin antigen

Factors such as developmental stage or physiological and infectious stress may change patterns of post-translational protein modification. In order to determine whether such regulated types of modification may influence T cell responsiveness to self proteins we examined the T cell response of SJL (H...

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Veröffentlicht in:International immunology 1998, Vol.10 (7), p.943-950
Hauptverfasser: Van Stipdonk, MJB, Willems, A A, Amor, S, Persoon-Deen, C, Travers, P J, Boog, CJP, Van Noort, JM
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container_end_page 950
container_issue 7
container_start_page 943
container_title International immunology
container_volume 10
creator Van Stipdonk, MJB
Willems, A A
Amor, S
Persoon-Deen, C
Travers, P J
Boog, CJP
Van Noort, JM
description Factors such as developmental stage or physiological and infectious stress may change patterns of post-translational protein modification. In order to determine whether such regulated types of modification may influence T cell responsiveness to self proteins we examined the T cell response of SJL (H-2 super(s)) mice to alpha B-crystallin, a small heat shock protein that can exist in differentially phosphorylated forms. Epitope mapping revealed the presence of two T cell epitopes that are presented by I-A super(s). One major epitope including residues 41-56 contains an amino acid residue (Ser45) that can be phosphorylated as the result of aging or stress. Accordingly, T cells from SJL mice discriminate between preparations of alpha B-crystallin that differ in their extent of phosphorylation at the level of whole protein as well as at the level of determinant-specific responses. Phosphorylation at Ser45 does not prevent binding of the peptide 41-56 to I-A super(s) and computer-assisted modelling of the peptide-MHC complex suggests that the phosphate group of the bound peptide extends outwards from the peptide-binding cleft and may thus be available for direct contact with TCR. Together, our data provide evidence that stress-inducible phosphorylation of alpha B-crystallin creates neo-determinants for T cells and, therefore, may contribute to the breakdown of peripheral tolerance to this self protein.
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Phosphorylation at Ser45 does not prevent binding of the peptide 41-56 to I-A super(s) and computer-assisted modelling of the peptide-MHC complex suggests that the phosphate group of the bound peptide extends outwards from the peptide-binding cleft and may thus be available for direct contact with TCR. 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title T cells discriminate between differentially phosphorylated forms of alpha B-crystallin, a major central nervous system myelin antigen
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