Authors
Michael Harrison, Paul E Chappell, Samer Halabi, Maria Danysz, Enock M Mararo, Lukasz Magiera, Clemens Hermann, Michael J Deery, Kathryn S Lilley, Hans-Joachim Wallny, David W Avila, William Mwangi, Venugopal Nair, Susan M Lea, Nicola Ternette, Jim Kaufman
Published in
eLife. Volume 15. Nov 02, 2026. Epub Nov 02, 2026.
Abstract
In chickens and humans, classical class I molecules of the major histocompatibility complex (MHC) have a spectrum of correlated properties, including cell surface expression and peptide repertoire. Understanding the impact of these promiscuous generalists and fastidious specialists is of considerable interest. The promiscuous BF2 molecule from the chicken B21 haplotype, BF2*21:01, binds a wide range of peptides by remodelling the peptide-binding site, allowing co-variation of the anchor residues at peptide positions P2 and Pc-2, and binding of an anchor residue at Pc. Using in vitro refolding assays with peptides and peptide libraries, determining thermostability and crystal structures, and analysing a chicken B21 cell line by immunopeptidomics, we found that BF2*21:01 will accommodate many possible combinations at P2 and Pc-2, as well as several hydrophobic amino acids at Pc. However, marked preferences for particular peptide lengths, particular amino acids at the three anchor residues, and particular combinations of amino acids at P2 and Pc-2 as well as at P3 and Pc-3 together lead to high frequencies of major peptides while still allowing the possibility of presenting a wide peptide repertoire. These simplifying principles may eventually allow predictions of pathogen peptides with stable binding for this iconic promiscuous class I molecule, as well as providing the data for more sophisticated peptide prediction methods.
PMID:
42970346
Bibliographic data and abstract were imported from PubMed on 03 Nov 2026.
Read full publication at:
Please sign in
to see all details.
Advertisement
Stats
- Recommendations n/a n/a positive of 0 vote(s)
- Views 5
- Comments 0