Your browser version may not work well with NCBI's Web applications. More information here...
1: J Immunol. 2006 Mar 1;176(5):2697-701.
Related Articles, Links
Click here to read Click here to read
Cutting edge: HLA-B27 acquires many N-terminal dibasic peptides: coupling cytosolic peptide stability to antigen presentation.

Herberts CA, Neijssen JJ, de Haan J, Janssen L, Drijfhout JW, Reits EA, Neefjes JJ.

Division of Tumor Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands.

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.

Publication Types:
PMID: 16493024 [PubMed - indexed for MEDLINE]