Definition of the peptide binding motif within DRB1*1401 restricted epitopes by peptide competition and structural modeling.

Abstract:

:This study identified the peptide-binding motif of HLA-DRA/DRB1*1401 (DR1401). First, peptides containing DR1401 restricted epitopes were identified using tetramer-guided epitope mapping. Among these, an influenza B peptide was selected for the motif study. After confirming the binding register for this peptide using a set of arginine substitutions, binding affinities were determined for 33 peptides derived from this influenza B sequence with single amino acid substitutions. The DR1401 peptide-binding motif was deduced from the relative binding affinities of these peptides and confirmed by structural modeling. Pocket 1 demonstrated a preference for aliphatic anchor residues and methionine. Pocket 4 accommodated methionine and aliphatic residues, but also allowed some polar and charged amino acids. Pocket 6 preferred basic residues but also allowed some polar and aliphatic amino acids. Pocket 9 preferred aliphatic and aromatic amino acids and tolerated some polar residues but excluded all charged residues. Together these preferences define a distinct set of peptides that can be presented by DR1401. The resulting motif was used to verify T cell epitopes within the novel antigenic peptides identified by tetramer-guided epitope mapping and within peptides from published reports that contain putative DR1401 epitopes.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

James EA,Moustakas AK,Berger D,Huston L,Papadopoulos GK,Kwok WW

doi

10.1016/j.molimm.2007.12.013

subject

Has Abstract

pub_date

2008-05-01 00:00:00

pages

2651-9

issue

9

eissn

0161-5890

issn

1872-9142

pii

S0161-5890(07)00897-8

journal_volume

45

pub_type

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