In silico characterization of immunogenic epitopes presented by HLA-Cw*0401

Joo Chuan Tong, Zong Hong Zhang, J. Thomas August, Vladimir Brusic, Tin Wee Tan, Shoba Ranganathan*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    13 Citations (Scopus)
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    Background: HLA-C locus products are poorly understood in part due to their low expression at the cell surface. Recent data indicate that these molecules serve as major restriction elements for human immunodeficiency virus type I (HIV-I) cytotoxic T lymphocyte (CTL) epitopes. We report here a structure-based technique for the prediction of peptides binding to Cw*0401. The models were rigorously trained, tested and validated using experimentally verified Cw*0401 binding and non-binding peptides obtained from biochemical studies. A new scoring scheme facilitates the identification of immunological hot spots within antigens, based on the sum of predicted binding energies of the top four binders within a window of 30 amino acids. Results: High predictivity is achieved when tested on the training (r2 = 0.88, s = 3.56 kj/mol, q2 = 0.84, Spress = 5.18 kj/mol) and test (AROC = 0.93) datasets. Characterization of the predicted Cw*0401 binding sequences indicate that amino acids at key anchor positions share common physico-chemical properties which correlate well with existing experimental studies. Conclusion: The analysis of predicted Cw*0401 -binding peptides showed that anchor residues may not be restrictive and the Cw*0401 binding pockets may possibly accommodate a wide variety of peptides with common physico-chemical properties. The potential Cw*0401-specific T-cell epitope repertoires for HIV-I p24gag and gp160gag glycoproteins are well distributed throughout both glycoproteins, with thirteen and nine immunological hot spots for HIV-I p24gag and gp 160gag glycoproteins respectively. These findings provide new insights into HLA-C peptide selectivity, indicating that pre-selection of candidate HLA-C peptides may occur at the TAP level, prior to peptide loading in the endoplasmic reticulum.

    Original languageEnglish
    Article number7
    Pages (from-to)1-8
    Number of pages8
    JournalImmunome Research
    Issue number1
    Publication statusPublished - 2007

    Bibliographical note

    Copyright 2007 Tong et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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