Effect of secondary anchor amino acid substitutions on the immunogenic properties of an HLA-A*0201-restricted T cell epitope derived from the Trypanosoma cruzi KMP-11 protein
Peptides, ISSN: 0196-9781, Vol: 78, Page: 68-76
2016
- 7Citations
- 34Captures
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Metrics Details
- Citations7
- Citation Indexes7
- CrossRef7
- Captures34
- Readers34
- 34
Article Description
The TcTLE peptide (TLEEFSAKL) is a CD8 + T cell HLA-A*0201-restricted epitope derived from the Trypanosoma cruzi KMP-11 protein that is efficiently processed, presented and recognized by CD8 + T cells from chagasic patients. Since the immunogenic properties of wild-type epitopes may be enhanced by suitable substitutions in secondary anchor residues, we have studied the effect of introducing specific mutations at position 3, 6 and 7 of the TcTLE peptide. Mutations (E3L, S6V and A7F) were chosen on the basis of in silico predictions and in vitro assays were performed to determine the TcTLE-modified peptide binding capacity to the HLA-A*0201 molecule. In addition, the functional activity of peptide-specific CD8 + T cells in HLA-A2 + chagasic patients was also interrogated. In contrast to bioinformatics predictions, the TcTLE-modified peptide was found to have lower binding affinity and stability than the original peptide. Nevertheless, CD8 + T cells from chronic chagasic patients recognized the TcTLE-modified peptide producing TNF-α and INF-γ and expressing CD107a/b, though in less extension than the response triggered by the original peptide. Overall, although the amino acids at positions 3, 6 and 7 of TcTLE are critical for the peptide affinity, they have a limited effect on the immunogenic properties of the TcTLE epitope.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0196978116300183; http://dx.doi.org/10.1016/j.peptides.2016.02.002; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84958818127&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/26854383; https://linkinghub.elsevier.com/retrieve/pii/S0196978116300183; https://dx.doi.org/10.1016/j.peptides.2016.02.002
Elsevier BV
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