Conversion of a self peptide sequence into a Kd-restricted neo-antigen by a Tyr substitution.

Détails

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Accès restreint UNIL
Etat: Public
Version: Final published version
Licence: Non spécifiée
ID Serval
serval:BIB_0D20366C5661
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Conversion of a self peptide sequence into a Kd-restricted neo-antigen by a Tyr substitution.
Périodique
The Journal of experimental medicine
Auteur⸱e⸱s
Healy F., Drouet C., Romero P., Jaulin C., Maryanski J.L.
ISSN
0022-1007
ISSN-L
0022-1007
Statut éditorial
Publié
Date de publication
01/12/1991
Peer-reviewed
Oui
Volume
174
Numéro
6
Pages
1657-1660
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
We have previously found that a Tyr residue was critical for the interaction of peptides with the Kd molecule, and therefore may be acting as an anchor residue. In the present report we show that it is possible to convert a self peptide sequence into a Kd-restricted neo-antigen by a single Tyr substitution at position 2 of the peptide. This supports the idea that Tyr is a critical element in the binding motif of Kd-restricted peptides and is a finding that could also prove useful for vaccine development.
Mots-clé
Amino Acid Sequence, Animals, H-2 Antigens/immunology, Immunization, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Molecular Sequence Data, Peptides/immunology, Structure-Activity Relationship, T-Lymphocytes, Cytotoxic/immunology, Tyrosine
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/01/2008 12:27
Dernière modification de la notice
09/08/2024 15:52
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