A new unconventional HLA-A2-restricted epitope from HBV core protein elicits antiviral cytotoxic T lymphocytes
Protein & Cell
; (12): 317-327, 2014.
Article
in En
| WPRIM
| ID: wpr-757497
Responsible library:
WPRO
ABSTRACT
Cytotoxic T cells (CTLs) play a key role in the control of Hepatitis B virus (HBV) infection and viral clearance. However, most of identified CTL epitopes are derived from HBV of genotypes A and D, and few have been defined in virus of genotypes B and C which are more prevalent in Asia. As HBV core protein (HBc) is the most conservative and immunogenic component, in this study we used an overlapping 9-mer peptide pool covering HBc to screen and identify specific CTL epitopes. An unconventional HLA-A2-restricted epitope HBc141-149 was discovered and structurally characterized by crystallization analysis. The immunogenicity and anti-HBV activity were further determined in HBV and HLA-A2 transgenic mice. Finally, we show that mutations in HBc141-149 epitope are associated with viral parameters and disease progression in HBV infected patients. Our data therefore provide insights into the structure characteristics of this unconventional epitope binding to MHC-I molecules, as well as epitope specific CTL activity that orchestrate T cell response and immune evasion in HBV infected patients.
Full text:
1
Index:
WPRIM
Main subject:
Protein Binding
/
Binding Sites
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Mice, Transgenic
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T-Lymphocytes, Cytotoxic
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HLA-A2 Antigen
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Chemistry
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Hepatitis B virus
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Amino Acid Sequence
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Protein Structure, Tertiary
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Allergy and Immunology
Type of study:
Prognostic_studies
Limits:
Animals
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Female
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Humans
/
Male
Language:
En
Journal:
Protein & Cell
Year:
2014
Type:
Article