| Autor: |
Youngchang Kim, Natalia Maltseva, Christine Tesar, Robert Jedrzejczak, Michael Endres, Heng Ma, Haley L. Dugan, Christopher T. Stamper, Changsoo Chang, Lei Li, Siriruk Changrob, Nai-Ying Zheng, Min Huang, Arvind Ramanathan, Patrick Wilson, Karolina Michalska, Andrzej Joachimiak |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
iScience, Vol 27, Iss 2, Pp 108976- (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2589-0042 |
| DOI: |
10.1016/j.isci.2024.108976 |
| Popis: |
Summary: Coronavirus nucleocapsid protein (NP) of SARS-CoV-2 plays a central role in many functions important for virus proliferation including packaging and protecting genomic RNA. The protein shares sequence, structure, and architecture with nucleocapsid proteins from betacoronaviruses. The N-terminal domain (NPRBD) binds RNA and the C-terminal domain is responsible for dimerization. After infection, NP is highly expressed and triggers robust host immune response. The anti-NP antibodies are not protective and not neutralizing but can effectively detect viral proliferation soon after infection. Two structures of SARS-CoV-2 NPRBD were determined providing a continuous model from residue 48 to 173, including RNA binding region and key epitopes. Five structures of NPRBD complexes with human mAbs were isolated using an antigen-bait sorting. Complexes revealed a distinct complement-determining regions and unique sets of epitope recognition. This may assist in the early detection of pathogens and designing peptide-based vaccines. Mutations that significantly increase viral load were mapped on developed, full length NP model, likely impacting interactions with host proteins and viral RNA. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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