Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-019-53201-6
Title: Crystal structure of suboptimal viral fragments of Epstein Barr Virus Rta peptide-HLA complex that stimulate CD8 T cell response
Authors: Huan, X. 
Zhuo, Z.
Xiao, Z. 
Ren, E.C. 
Issue Date: 2019
Publisher: Nature Publishing Group
Citation: Huan, X., Zhuo, Z., Xiao, Z., Ren, E.C. (2019). Crystal structure of suboptimal viral fragments of Epstein Barr Virus Rta peptide-HLA complex that stimulate CD8 T cell response. Scientific Reports 9 (1) : 16660. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-019-53201-6
Rights: Attribution 4.0 International
Abstract: Peptides presented by Human leukocyte antigen (HLA) class-I molecules are generally 8–10 amino acids in length. However, the predominant pool of peptide fragments generated by proteasomes is less than 8 amino acids in length. Using the Epstein - Barr virus (EBV) Rta-epitope (ATIGTAMYK, residues 134–142) restricted by HLA-A*11:01 which generates a strong immunodominant response, we investigated the minimum length of a viral peptide that can constitute a viral epitope recognition by CD8 T cells. The results showed that Peripheral blood mononuclear cells (PBMCs) from healthy donors can be stimulated by a viral peptide fragment as short as 4-mer (AMYK), together with a 5-mer (ATIGT) to recapitulate the full length EBV Rta epitope. This was confirmed by generating crystals of the tetra-complex (2 peptides, HLA and ?2-microglobulin). The solved crystal structure of HLA-A*11:01 in complex with these two short peptides revealed that they can bind in the same orientation similar to parental peptide (9-mer) and the free ends of two short peptides acquires a bulged conformation that is directed towards the T cell receptor. Our data shows that suboptimal length of 4-mer and 5-mer peptides can complement each other to form a stable peptide-MHC (pMHC) complex. © 2019, The Author(s).
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/212751
ISSN: 20452322
DOI: 10.1038/s41598-019-53201-6
Rights: Attribution 4.0 International
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