Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-017-05171-w
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dc.titleDual non-contiguous peptide occupancy of HLA class i evoke antiviral human CD8 T cell response and form neo-epitopes with self-antigens /631/250/21/324/1509 /631/326/596/1553 /13/31 /13/106 /13/109 /145 /82/83 article
dc.contributor.authorXiao, Z
dc.contributor.authorYe, Z
dc.contributor.authorTadwal, V.S
dc.contributor.authorShen, M
dc.contributor.authorRen, E.C
dc.date.accessioned2020-10-20T09:11:02Z
dc.date.available2020-10-20T09:11:02Z
dc.date.issued2017
dc.identifier.citationXiao, Z, Ye, Z, Tadwal, V.S, Shen, M, Ren, E.C (2017). Dual non-contiguous peptide occupancy of HLA class i evoke antiviral human CD8 T cell response and form neo-epitopes with self-antigens /631/250/21/324/1509 /631/326/596/1553 /13/31 /13/106 /13/109 /145 /82/83 article. Scientific Reports 7 (1) : 5072. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-017-05171-w
dc.identifier.issn20452322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/178315
dc.description.abstractHost CD8 T cell response to viral infections involves recognition of 8-10-mer peptides presented by MHC-I molecules. However, proteasomes generate predominantly 2-7-mer peptides, but the role of these peptides is largely unknown. Here, we show that single short peptides of <8-mer from Latent Membrane Protein 2 (LMP2) of Epstein Barr Virus (EBV) can bind HLA-A?11:01 and stimulate CD8+ cells. Surprisingly, two peptide fragments between 4-7-mer derived from LMP2(340-349) were able to complement each other, forming combination epitopes that can stimulate specific CD8+ T cell responses. Moreover, peptides from self-antigens can complement non-self peptides within the HLA binding cleft, forming neoepitopes. Solved structures of a tetra-complex comprising two peptides, HLA and ?2-microglobulin revealed the free terminals of the two peptides to adopt an upward conformation directed towards the T cell receptor. Our results demonstrate a previously unknown mix-and-match combination of dual peptide occupancy in HLA that can generate vast combinatorial complexity. © 2017 The Author(s).
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectantivirus agent
dc.subjectautoantigen
dc.subjectepitope
dc.subjectHLA antigen class 1
dc.subjectlymphocyte antigen receptor
dc.subjectpeptide
dc.subjectallele
dc.subjectamino acid sequence
dc.subjectbinding site
dc.subjectCD8+ T lymphocyte
dc.subjectchemistry
dc.subjecthuman
dc.subjectimmunology
dc.subjectlymphocyte activation
dc.subjectmetabolism
dc.subjectprotein stability
dc.subjectstatic electricity
dc.subjectAlleles
dc.subjectAmino Acid Sequence
dc.subjectAntiviral Agents
dc.subjectAutoantigens
dc.subjectBinding Sites
dc.subjectCD8-Positive T-Lymphocytes
dc.subjectEpitopes
dc.subjectHistocompatibility Antigens Class I
dc.subjectHumans
dc.subjectLymphocyte Activation
dc.subjectPeptides
dc.subjectProtein Stability
dc.subjectReceptors, Antigen, T-Cell, alpha-beta
dc.subjectStatic Electricity
dc.typeArticle
dc.contributor.departmentDEPT OF MICROBIOLOGY & IMMUNOLOGY
dc.description.doi10.1038/s41598-017-05171-w
dc.description.sourcetitleScientific Reports
dc.description.volume7
dc.description.issue1
dc.description.page5072
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