Abstract:
:Peptides bind MHC class I molecules by anchoring hydrophobic side chains into pockets in the peptide binding groove. Here, we report an immunogenic (in vitro and in vivo) MUC1 glycopeptide (MUC1-8-5GalNAc) bound to H-2Kb, fully crossreactive with the nonglycosylated variant. Molecular modeling showed that the central P5-Thr-GalNAc residue points into the C pocket and forms van der Waals and hydrogen bond interactions with the MHC class I. As predicted, GalNAc, a modified peptide carrying an additional anchor in the central C anchor pocket, increased the affinity by approximately 100-fold compared with the native low-affinity peptide (MUC1-8). The findings demonstrate that glycopeptides associated with MHC class I molecules can use GalNAc to anchor the peptide in the groove and enable high-affinity binding.
journal_name
Proc Natl Acad Sci U S Aauthors
Apostolopoulos V,Yuriev E,Ramsland PA,Halton J,Osinski C,Li W,Plebanski M,Paulsen H,McKenzie IFdoi
10.1073/pnas.2432220100keywords:
subject
Has Abstractpub_date
2003-12-09 00:00:00pages
15029-34issue
25eissn
0027-8424issn
1091-6490pii
2432220100journal_volume
100pub_type
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