Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies
SARS-CoV-2 virus has become the centre of virology research since the outbreak of COVID-19. Many studies have been done on the viral structure and properties. It was discovered that spike protein mediates critical functions of viral attachment to host cells and membrane fusion, rendering it an impor...
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| Format: | Final Year Project (FYP) |
| Language: | English |
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Nanyang Technological University
2024
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| Online Access: | https://hdl.handle.net/10356/176677 |
| _version_ | 1826120951682564096 |
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| author | Wu, Yanjun |
| author2 | Richard J Sugrue |
| author_facet | Richard J Sugrue Wu, Yanjun |
| author_sort | Wu, Yanjun |
| collection | NTU |
| description | SARS-CoV-2 virus has become the centre of virology research since the outbreak of COVID-19. Many studies have been done on the viral structure and properties. It was discovered that spike protein mediates critical functions of viral attachment to host cells and membrane fusion, rendering it an important target for therapeutic development. This project aims to analyse the spike protein by focusing on its interaction with four human monoclonal antibodies (PD4, PD5, SC23, SC29). The purpose is to first determine which part of the S protein these antibodies specifically bind to, and use them to monitor the process of spike protein synthesis, modification, and export onto the cell surface. The main method used was immunofluorescence assay done in transfected Vero-E6 cells expressing recombinant spike protein. It is revealed that a key conformation is formed in S1 subunit when spike protein undergoes post-translational modification in Golgi apparatus, and this conformation is targeted by neutralising antibodies. Notably, S1 subunit can be displayed on the cell surface independently without S2 subunit, enabling it to serve as a potential means of immunity escape by seizing the neutralising antibodies away from full-length spike proteins. These conclusions highlight the importance of targeting S1 in therapeutic development. |
| first_indexed | 2024-10-01T05:24:50Z |
| format | Final Year Project (FYP) |
| id | ntu-10356/176677 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T05:24:50Z |
| publishDate | 2024 |
| publisher | Nanyang Technological University |
| record_format | dspace |
| spelling | ntu-10356/1766772024-05-20T15:33:19Z Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies Wu, Yanjun Richard J Sugrue School of Biological Sciences RJSugrue@ntu.edu.sg Medicine, Health and Life Sciences SARS-CoV-2 Virus Fusion protein SARS-CoV-2 virus has become the centre of virology research since the outbreak of COVID-19. Many studies have been done on the viral structure and properties. It was discovered that spike protein mediates critical functions of viral attachment to host cells and membrane fusion, rendering it an important target for therapeutic development. This project aims to analyse the spike protein by focusing on its interaction with four human monoclonal antibodies (PD4, PD5, SC23, SC29). The purpose is to first determine which part of the S protein these antibodies specifically bind to, and use them to monitor the process of spike protein synthesis, modification, and export onto the cell surface. The main method used was immunofluorescence assay done in transfected Vero-E6 cells expressing recombinant spike protein. It is revealed that a key conformation is formed in S1 subunit when spike protein undergoes post-translational modification in Golgi apparatus, and this conformation is targeted by neutralising antibodies. Notably, S1 subunit can be displayed on the cell surface independently without S2 subunit, enabling it to serve as a potential means of immunity escape by seizing the neutralising antibodies away from full-length spike proteins. These conclusions highlight the importance of targeting S1 in therapeutic development. Bachelor's degree 2024-05-20T02:27:18Z 2024-05-20T02:27:18Z 2024 Final Year Project (FYP) Wu, Y. (2024). Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/176677 https://hdl.handle.net/10356/176677 en application/pdf Nanyang Technological University |
| spellingShingle | Medicine, Health and Life Sciences SARS-CoV-2 Virus Fusion protein Wu, Yanjun Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title | Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title_full | Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title_fullStr | Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title_full_unstemmed | Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title_short | Analysis of surface expressed recombinant SARS-CoV-2 spike protein using human monoclonal antibodies |
| title_sort | analysis of surface expressed recombinant sars cov 2 spike protein using human monoclonal antibodies |
| topic | Medicine, Health and Life Sciences SARS-CoV-2 Virus Fusion protein |
| url | https://hdl.handle.net/10356/176677 |
| work_keys_str_mv | AT wuyanjun analysisofsurfaceexpressedrecombinantsarscov2spikeproteinusinghumanmonoclonalantibodies |