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T cell recognition of the dominant I-A(k)-restricted hen egg lysozyme epitope: critical role for asparagine deamidation

McAdam, Stephen N.; Fleckenstein, Burkhard; Rasmussen, Ingunn B; Sandlie, Inger; Bogen, Bjarne; Vinter, N.J.; Sollid, Ludvig Magne
Journal article; PublishedVersion; Peer reviewed
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76.+010113.pdf (101.0Kb)
Year
2001
Permanent link
http://urn.nb.no/URN:NBN:no-57782

CRIStin
438500

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Appears in the following Collection
  • Biologisk institutt [118]
  • Institutt for klinisk medisin [7752]
  • CRIStin høstingsarkiv [22471]
Original version
Journal of Experimental Medicine. 2001, 193 (11), 1239-1246
Abstract
Type-B T cells raised against the immunodominant peptide in hen egg lysozyme (HEL(48-62)) do not respond to whole lysozyme, and this has been thought to indicate that peptide can bind to I-A(k) in different conformations. Here we demonstrate that such T cells recognize a deamidated form of the HEL peptide and not the native peptide. The sequence of the HEL epitope facilitates rapid and spontaneous deamidation when present as a free peptide or within a flexible domain. However, this deamidated epitope is not created within intact lysozyme, most likely because it resides in a highly structured part of the protein. These findings argue against the existence of multiple conformations of the same peptide-MHC complex and have important implications for the design of peptide-based vaccines. Furthermore, as the type-B T cells are known to selectively evade induction of tolerance when HEL is expressed as a transgene, these results suggest that recognition of posttranslationally modified self-antigen may play a role in autoimmunity.

This research was originally published in: Journal of Experimental Medicine. © Rockefeller University Press.
 
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