Article ; Online: Inside-out: Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9.
2023 Volume 18, Issue 4, Page(s) e0283194
Abstract: Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12's nucleotidylation activity while also serving to recruit proteins required for viral 5'-capping. Anti-nsp9 ... ...
Abstract | Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12's nucleotidylation activity while also serving to recruit proteins required for viral 5'-capping. Anti-nsp9 specific nanobodies have been isolated previously. We confirm that their binding mode is centred upon Trp-53 within SARS-CoV-2 nsp9. Antibody binding at this site surprisingly results in large-scale changes to the overall topology of this coronaviral unique fold. We further characterise the antibody-induced structural dynamism within nsp9, identifying a number of potentially flexible regions. A large expansion of the cavity between the s2-s3 and s4-s5 loops is particularly noteworthy. As is the potential for large-scale movements in the C-terminal GxxxG helix. |
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MeSH term(s) | Humans ; SARS-CoV-2/metabolism ; Viral Nonstructural Proteins/metabolism ; COVID-19 |
Chemical Substances | Viral Nonstructural Proteins |
Language | English |
Publishing date | 2023-04-10 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 2267670-3 |
ISSN | 1932-6203 ; 1932-6203 |
ISSN (online) | 1932-6203 |
ISSN | 1932-6203 |
DOI | 10.1371/journal.pone.0283194 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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