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  1. Article ; Online: Binding Studies of the Prodrug HAO472 to SARS-Cov‑2 Nsp9 and Variants

    Miaomiao Liu / Dene R. Littler / Jamie Rossjohn / Ronald J Quinn

    ACS Omega, Vol 7, Iss 8, Pp 7327-

    2022  Volume 7332

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Inside-out

    Yue Pan / Indu R Chandrashekaran / Luke Tennant / Jamie Rossjohn / Dene R Littler

    PLoS ONE, Vol 18, Iss 4, p e

    Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9.

    2023  Volume 0283194

    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.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Inside-out

    Yue Pan / Indu R. Chandrashekaran / Luke Tennant / Jamie Rossjohn / Dene R. Littler

    PLoS ONE, Vol 18, Iss

    Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9

    2023  Volume 4

    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.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9

    Dene R. Littler / Benjamin S. Gully / Rhys N. Colson / Jamie Rossjohn

    iScience, Vol 23, Iss 7, Pp 101258- (2020)

    2020  

    Abstract: Summary: Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and ... ...

    Abstract Summary: Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and viral genomic RNA reproduction. We sought to better characterize the SARS-CoV-2 Nsp9 and subsequently solved its X-ray crystal structure, in an apo form and, unexpectedly, in a peptide-bound form with a sequence originating from a rhinoviral 3C protease sequence (LEVL). The SARS-CoV-2 Nsp9 structure revealed the high level of structural conservation within the Nsp9 family. The exogenous peptide binding site is close to the dimer interface and impacted the relative juxtapositioning of the monomers within the homodimer. We have established a protocol for the production of SARS-CoV-2 Nsp9, determined its structure, and identified a peptide-binding site that warrants further study to understanding Nsp9 function.
    Keywords Virology ; Structural Biology ; Protein Structure Aspects ; 3D Reconstruction of Protein ; Science ; Q ; covid19
    Language English
    Publishing date 2020-07-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: OZITX, a pertussis toxin-like protein for occluding inhibitory G protein signalling including Gαz

    Alastair C. Keen / Maria Hauge Pedersen / Laura Lemel / Daniel J. Scott / Meritxell Canals / Dene R. Littler / Travis Beddoe / Yuki Ono / Lei Shi / Asuka Inoue / Jonathan A. Javitch / J. Robert Lane

    Communications Biology, Vol 5, Iss 1, Pp 1-

    2022  Volume 10

    Abstract: A recently identified pertussis toxin-like AB5 toxin, OZITX, is found to inhibit Gαi/o and Gαz G proteins. In combination with directed mutations, it is a useful tool for interrogating Gαi/o/z G protein subunits individually. ...

    Abstract A recently identified pertussis toxin-like AB5 toxin, OZITX, is found to inhibit Gαi/o and Gαz G proteins. In combination with directed mutations, it is a useful tool for interrogating Gαi/o/z G protein subunits individually.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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