Structural and Biophysical Insights into the TCRαβ Complex in Chickens
Summary: In this work, chicken HPAIV H5N1 epitope-specific TCRαβ (ch-TCRαβ) was isolated and its structure was determined. The Cα domain of ch-TCRαβ does not exhibit the typical structure of human TCRαβ, and the DE loop extends outward, resulting in close proximity between the Cα domain of ch-TCRαβ...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004220310257 |
| _version_ | 1818595867734573056 |
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| author | Lijie Zhang Yanjie Liu Geng Meng Ruiying Liang Bing Zhang Chun Xia |
| author_facet | Lijie Zhang Yanjie Liu Geng Meng Ruiying Liang Bing Zhang Chun Xia |
| author_sort | Lijie Zhang |
| collection | DOAJ |
| description | Summary: In this work, chicken HPAIV H5N1 epitope-specific TCRαβ (ch-TCRαβ) was isolated and its structure was determined. The Cα domain of ch-TCRαβ does not exhibit the typical structure of human TCRαβ, and the DE loop extends outward, resulting in close proximity between the Cα domain of ch-TCRαβ and CD3εδ/γ. The FG loop of the Cβ domain of ch-TCRαβ is shorter. The changes in the C domains of ch-TCRαβ and the difference in chicken CD3εδ/γ confirm that the complexes formed by TCRαβ and CD3εδ/γ differ from those in humans. In the chicken complex, a positively charged cleft is formed between the two CDR3 loops that might accommodate the acidic side chains of the chicken pMHC-I-bound HPAIV epitope intermediate portion oriented toward ch-TCRαβ. This is the first reported structure of chicken TCRαβ, and it provides a structural model of the ancestral TCR system in the immune synapses between T cells and antigen-presenting cells in lower vertebrates. |
| first_indexed | 2024-12-16T11:22:50Z |
| format | Article |
| id | doaj.art-9e3887f332d24b97a19fe557fa55b39e |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-12-16T11:22:50Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-9e3887f332d24b97a19fe557fa55b39e2022-12-21T22:33:26ZengElsevieriScience2589-00422020-12-012312101828Structural and Biophysical Insights into the TCRαβ Complex in ChickensLijie Zhang0Yanjie Liu1Geng Meng2Ruiying Liang3Bing Zhang4Chun Xia5Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, China; Joint National Laboratory for Antibody Drug Engineering, Key Laboratory of Cell and Molecular Immunology, School of Medical Sciences, Henan University, Kaifeng 475004, ChinaDepartment of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, ChinaDepartment of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, ChinaDepartment of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, ChinaDepartment of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, ChinaDepartment of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Haidian District, Beijing 100193, China; Corresponding authorSummary: In this work, chicken HPAIV H5N1 epitope-specific TCRαβ (ch-TCRαβ) was isolated and its structure was determined. The Cα domain of ch-TCRαβ does not exhibit the typical structure of human TCRαβ, and the DE loop extends outward, resulting in close proximity between the Cα domain of ch-TCRαβ and CD3εδ/γ. The FG loop of the Cβ domain of ch-TCRαβ is shorter. The changes in the C domains of ch-TCRαβ and the difference in chicken CD3εδ/γ confirm that the complexes formed by TCRαβ and CD3εδ/γ differ from those in humans. In the chicken complex, a positively charged cleft is formed between the two CDR3 loops that might accommodate the acidic side chains of the chicken pMHC-I-bound HPAIV epitope intermediate portion oriented toward ch-TCRαβ. This is the first reported structure of chicken TCRαβ, and it provides a structural model of the ancestral TCR system in the immune synapses between T cells and antigen-presenting cells in lower vertebrates.http://www.sciencedirect.com/science/article/pii/S2589004220310257ImmunologyStructural Biology |
| spellingShingle | Lijie Zhang Yanjie Liu Geng Meng Ruiying Liang Bing Zhang Chun Xia Structural and Biophysical Insights into the TCRαβ Complex in Chickens iScience Immunology Structural Biology |
| title | Structural and Biophysical Insights into the TCRαβ Complex in Chickens |
| title_full | Structural and Biophysical Insights into the TCRαβ Complex in Chickens |
| title_fullStr | Structural and Biophysical Insights into the TCRαβ Complex in Chickens |
| title_full_unstemmed | Structural and Biophysical Insights into the TCRαβ Complex in Chickens |
| title_short | Structural and Biophysical Insights into the TCRαβ Complex in Chickens |
| title_sort | structural and biophysical insights into the tcrαβ complex in chickens |
| topic | Immunology Structural Biology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004220310257 |
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