ArticleMolecular immunology2008
Definition of the peptide binding motif within DRB1*1401 restricted epitopes by peptide competition and structural modeling.
Article in Molecular immunology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Osteoclasts in the Inflammatory Arthritis: Implications for Pathologic Osteolysis.Immune network · 2019Review
- Article
- Immune recognition of citrullinated epitopes.Immunology · 2016Review
- In Silico Identification of Highly Conserved Epitopes of Influenza A H1N1, H2N2, H3N2, and H5N1 with Diagnostic and Vaccination Potential.BioMed research international · 2015Article
- Immunodominant CD4+ T-cell responses to influenza A virus in healthy individuals focus on matrix 1 and nucleoprotein.Journal of virology · 2014Article
- DRB1*12:01 presents a unique subset of epitopes by preferring aromatics in pocket 9.Molecular immunology · 2012Article
- Papillomavirus-specific CD4+ T cells exhibit reduced STAT-5 signaling and altered cytokine profiles in patients with recurrent respiratory papillomatosis.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- T-cell responses in two unrelated hemophilia A inhibitor subjects include an epitope at the factor VIII R593C missense site.Journal of thrombosis and haemostasis : JTH · 2011Article
- The binding of antigenic peptides to HLA-DR is influenced by interactions between pocket 6 and pocket 9.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
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Authors and funding
6 authors.
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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.
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