Cutting edge: HLA-B27 acquires many N-terminal dibasic peptides: coupling cytosolic peptide stability to antigen presentation.
J Immunol
; 176(5): 2697-701, 2006 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-16493024
ABSTRACT
Ag presentation by MHC class I is a highly inefficient process because cytosolic peptidases destroy most peptides after proteasomal generation. Various mechanisms shape the MHC class I peptidome. We define a new one intracellular peptide stability. Peptides with two N-terminal basic amino acids are more stable than other peptides. Such peptides should be overrepresented in the peptidome of MHC class I-associated peptides. HLA-B27 binding peptides use anchor residue R at P2 and, although most amino acids are allowed, particular amino acids are overrepresented at P1, including R and K. We show that such N-terminal dibasic peptides are indeed more efficiently presented by HLA-B27. This suggests that HLA-B27 can present peptides from Ags present in fewer copies than required for successful peptide generation for other MHC class I molecules.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Antígeno HLA-B27
/
Apresentação de Antígeno
/
Citosol
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article