The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development
Foot-and-mouth disease virus (FMDV) poses a significant threat to the livestock industry. Through their recognition of the conserved epitopes presented by the swine leukocyte antigen (SLA), T cells play a pivotal role in the antiviral immunity of pigs. Herein, based on the peptide binding motif of S...
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2022-12-01
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author | Lei Feng Yong-Yu Gao Mingwei Sun Zi-Bin Li Qiang Zhang Jie Yang Cui Qiao Hang Jin Hong-Sheng Feng Yu-Han Xian Jianxun Qi George F. Gao William J. Liu Feng-Shan Gao |
author_facet | Lei Feng Yong-Yu Gao Mingwei Sun Zi-Bin Li Qiang Zhang Jie Yang Cui Qiao Hang Jin Hong-Sheng Feng Yu-Han Xian Jianxun Qi George F. Gao William J. Liu Feng-Shan Gao |
author_sort | Lei Feng |
collection | DOAJ |
description | Foot-and-mouth disease virus (FMDV) poses a significant threat to the livestock industry. Through their recognition of the conserved epitopes presented by the swine leukocyte antigen (SLA), T cells play a pivotal role in the antiviral immunity of pigs. Herein, based on the peptide binding motif of SLA-2*HB01, from an original SLA-2 allele, a series of functional T-cell epitopes derived from the dominant antigen VP1 of FMDV with high binding capacity to SLA-2 were identified. Two parallel peptides, Hu64 and As64, from the O and Asia I serotypes, respectively, were both crystallized with SLA-2*HB01. Compared to SLA-1 and SLA-3, the SLA-2 structures showed the flexibility of residues in the P4, P6, and P8 positions and in their potential interface with TCR. Notably, the peptides Hu64 and As64 adopted quite similar overall conformation when bound to SLA-2*HB01. Hu64 has two different conformations, a more stable ‘chair’ conformation and an unstable ‘boat’ conformation observed in the two molecules of one asymmetric unit, whereas only a single ‘chair’ conformation was observed for As64. Both Hu64 and As64 could induce similar dominant T-cell activities. Our interdisciplinary study establishes a basis for the in-depth interpretation of the peptide presentation of SLA-I, which can be used toward the development of universal vaccines. |
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spelling | doaj.art-b7db0303f064419f92ef0c67685c78f72023-11-24T13:54:23ZengMDPI AGCells2073-44092022-12-011124401710.3390/cells11244017The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine DevelopmentLei Feng0Yong-Yu Gao1Mingwei Sun2Zi-Bin Li3Qiang Zhang4Jie Yang5Cui Qiao6Hang Jin7Hong-Sheng Feng8Yu-Han Xian9Jianxun Qi10George F. Gao11William J. Liu12Feng-Shan Gao13Department of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaCAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing 100101, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaState Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaCAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing 100101, ChinaCAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing 100101, ChinaNHC Key Laboratory of Biosafety, Research Unit of Adaptive Evolution and Control of Emerging Viruses, Chinese Academy of Medical Sciences, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, ChinaDepartment of Bioengineering, College of Life and Health, Dalian University, Dalian 116622, ChinaFoot-and-mouth disease virus (FMDV) poses a significant threat to the livestock industry. Through their recognition of the conserved epitopes presented by the swine leukocyte antigen (SLA), T cells play a pivotal role in the antiviral immunity of pigs. Herein, based on the peptide binding motif of SLA-2*HB01, from an original SLA-2 allele, a series of functional T-cell epitopes derived from the dominant antigen VP1 of FMDV with high binding capacity to SLA-2 were identified. Two parallel peptides, Hu64 and As64, from the O and Asia I serotypes, respectively, were both crystallized with SLA-2*HB01. Compared to SLA-1 and SLA-3, the SLA-2 structures showed the flexibility of residues in the P4, P6, and P8 positions and in their potential interface with TCR. Notably, the peptides Hu64 and As64 adopted quite similar overall conformation when bound to SLA-2*HB01. Hu64 has two different conformations, a more stable ‘chair’ conformation and an unstable ‘boat’ conformation observed in the two molecules of one asymmetric unit, whereas only a single ‘chair’ conformation was observed for As64. Both Hu64 and As64 could induce similar dominant T-cell activities. Our interdisciplinary study establishes a basis for the in-depth interpretation of the peptide presentation of SLA-I, which can be used toward the development of universal vaccines.https://www.mdpi.com/2073-4409/11/24/4017SLA-2foot-and-mouth disease viruscrystalpeptideepitopeCTL |
spellingShingle | Lei Feng Yong-Yu Gao Mingwei Sun Zi-Bin Li Qiang Zhang Jie Yang Cui Qiao Hang Jin Hong-Sheng Feng Yu-Han Xian Jianxun Qi George F. Gao William J. Liu Feng-Shan Gao The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development Cells SLA-2 foot-and-mouth disease virus crystal peptide epitope CTL |
title | The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development |
title_full | The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development |
title_fullStr | The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development |
title_full_unstemmed | The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development |
title_short | The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development |
title_sort | parallel presentation of two functional ctl epitopes derived from the o and asia 1 serotypes of foot and mouth disease virus and swine sla 2 hb01 implications for universal vaccine development |
topic | SLA-2 foot-and-mouth disease virus crystal peptide epitope CTL |
url | https://www.mdpi.com/2073-4409/11/24/4017 |
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