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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: Multi-targeted loss of the antigen presentation molecule MR1 during HSV-1 and HSV-2 infection

    Carolyn Samer / Hamish E.G. McWilliam / Brian P. McSharry / Thilaga Velusamy / James G. Burchfield / Richard J. Stanton / David C. Tscharke / Jamie Rossjohn / Jose A. Villadangos / Allison Abendroth / Barry Slobedman

    iScience, Vol 27, Iss 2, Pp 108801- (2024)

    2024  

    Abstract: Summary: The major histocompatibility complex (MHC), Class-I-related (MR1) molecule presents microbiome-synthesized metabolites to Mucosal-associated invariant T (MAIT) cells, present at sites of herpes simplex virus (HSV) infection. During HSV type 1 ( ... ...

    Abstract Summary: The major histocompatibility complex (MHC), Class-I-related (MR1) molecule presents microbiome-synthesized metabolites to Mucosal-associated invariant T (MAIT) cells, present at sites of herpes simplex virus (HSV) infection. During HSV type 1 (HSV-1) infection there is a profound and rapid loss of MR1, in part due to expression of unique short 3 protein. Here we show that virion host shutoff RNase protein downregulates MR1 protein, through loss of MR1 transcripts. Furthermore, a third viral protein, infected cell protein 22, also downregulates MR1, but not classical MHC-I molecules. This occurs early in the MR1 trafficking pathway through proteasomal degradation. Finally, HSV-2 infection results in the loss of MR1 transcripts, and intracellular and surface MR1 protein, comparable to that seen during HSV-1 infection. Thus HSV coordinates a multifaceted attack on the MR1 antigen presentation pathway, potentially protecting infected cells from MAIT cell T cell receptor-mediated detection at sites of primary infection and reactivation.
    Keywords Cell biology ; Immunology ; Virology ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2024-02-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: 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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  6. Article ; Online: CD1a promotes systemic manifestations of skin inflammation

    Clare S. Hardman / Yi-Ling Chen / Marcin Wegrecki / Soo Weei Ng / Robert Murren / Davinderpreet Mangat / John-Paul Silva / Rebecca Munro / Win Yan Chan / Victoria O’Dowd / Carl Doyle / Prashant Mori / Andy Popplewell / Jamie Rossjohn / Daniel Lightwood / Graham S. Ogg

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 18

    Abstract: Skin inflammation is often accompanied by systemic disease, yet the pathways that regulate this escalation are little known. Here authors show that transgenic expression of human CD1a in mice leads to the escalation of experimental skin inflammation and ... ...

    Abstract Skin inflammation is often accompanied by systemic disease, yet the pathways that regulate this escalation are little known. Here authors show that transgenic expression of human CD1a in mice leads to the escalation of experimental skin inflammation and systemic inflammatory disease, and the generalized symptoms could be alleviated by blocking antibodies developed against CD1a.
    Keywords Science ; Q
    Language English
    Publishing date 2022-12-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C

    Shoeib Moradi / Sanda Stankovic / Geraldine M. O’Connor / Phillip Pymm / Bruce J. MacLachlan / Camilla Faoro / Christelle Retière / Lucy C. Sullivan / Philippa M. Saunders / Jacqueline Widjaja / Shea Cox-Livingstone / Jamie Rossjohn / Andrew G. Brooks / Julian P. Vivian

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 11

    Abstract: KIR2DL2 and KIR2DL3 are two inhibitory members of the killer-cell immunoglobulin-like receptors (KIR) family that share a common HLA-I preference in binding HLA from the C1 group. However, it is still unclear to what extent binding and function is ... ...

    Abstract KIR2DL2 and KIR2DL3 are two inhibitory members of the killer-cell immunoglobulin-like receptors (KIR) family that share a common HLA-I preference in binding HLA from the C1 group. However, it is still unclear to what extent binding and function is equivalent between KIR2DL2 and 2DL3. Here, the authors present the crystal structures of KIR2DL2 and 2DL3 in complex with HLA-C*07:02 and observe differences in HLA-C recognition between KIR2DL2 and 2DL3, which correlates with differences in HLA-C binding preference as they show with mutagenesis and binding studies.
    Keywords Science ; Q
    Language English
    Publishing date 2021-04-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: T cell receptor recognition of hybrid insulin peptides bound to HLA-DQ8

    Mai T. Tran / Pouya Faridi / Jia Jia Lim / Yi Tian Ting / Goodluck Onwukwe / Pushpak Bhattacharjee / Claerwen M. Jones / Eleonora Tresoldi / Fergus J. Cameron / Nicole L. La Gruta / Anthony W. Purcell / Stuart I. Mannering / Jamie Rossjohn / Hugh H. Reid

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 13

    Abstract: Epitopes formed by fusion of more than one self peptide, such as proinsulin and other β cell proteins, can result in the formation of non-self hybrid peptides that can potentially trigger autoimmune responses. Here the authors show how TRBV5 + T cell ... ...

    Abstract Epitopes formed by fusion of more than one self peptide, such as proinsulin and other β cell proteins, can result in the formation of non-self hybrid peptides that can potentially trigger autoimmune responses. Here the authors show how TRBV5 + T cell receptors are geared towards recognition of HLA-DQ8 bound hybrid peptides in patients with type 1 diabetes.
    Keywords Science ; Q
    Language English
    Publishing date 2021-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: HLA-A*11:01-restricted CD8+ T cell immunity against influenza A and influenza B viruses in Indigenous and non-Indigenous people.

    Jennifer R Habel / Andrea T Nguyen / Louise C Rowntree / Christopher Szeto / Nicole A Mifsud / E Bridie Clemens / Liyen Loh / Weisan Chen / Steve Rockman / Jane Nelson / Jane Davies / Adrian Miller / Steven Y C Tong / Jamie Rossjohn / Stephanie Gras / Anthony W Purcell / Luca Hensen / Katherine Kedzierska / Patricia T Illing

    PLoS Pathogens, Vol 18, Iss 3, p e

    2022  Volume 1010337

    Abstract: HLA-A*11:01 is one of the most prevalent human leukocyte antigens (HLAs), especially in East Asian and Oceanian populations. It is also highly expressed in Indigenous people who are at high risk of severe influenza disease. As CD8+ T cells can provide ... ...

    Abstract HLA-A*11:01 is one of the most prevalent human leukocyte antigens (HLAs), especially in East Asian and Oceanian populations. It is also highly expressed in Indigenous people who are at high risk of severe influenza disease. As CD8+ T cells can provide broadly cross-reactive immunity to distinct influenza strains and subtypes, including influenza A, B and C viruses, understanding CD8+ T cell immunity to influenza viruses across prominent HLA types is needed to rationally design a universal influenza vaccine and generate protective immunity especially for high-risk populations. As only a handful of HLA-A*11:01-restricted CD8+ T cell epitopes have been described for influenza A viruses (IAVs) and epitopes for influenza B viruses (IBVs) were still unknown, we embarked on an epitope discovery study to define a CD8+ T cell landscape for HLA-A*11:01-expressing Indigenous and non-Indigenous Australian people. Using mass-spectrometry, we identified IAV- and IBV-derived peptides presented by HLA-A*11:01 during infection. 79 IAV and 57 IBV peptides were subsequently screened for immunogenicity in vitro with peripheral blood mononuclear cells from HLA-A*11:01-expressing Indigenous and non-Indigenous Australian donors. CD8+ T cell immunogenicity screening revealed two immunogenic IAV epitopes (A11/PB2320-331 and A11/PB2323-331) and the first HLA-A*11:01-restricted IBV epitopes (A11/M41-49, A11/NS1186-195 and A11/NP511-520). The immunogenic IAV- and IBV-derived peptides were >90% conserved among their respective influenza viruses. Identification of novel immunogenic HLA-A*11:01-restricted CD8+ T cell epitopes has implications for understanding how CD8+ T cell immunity is generated towards IAVs and IBVs. These findings can inform the development of rationally designed, broadly cross-reactive influenza vaccines to ensure protection from severe influenza disease in HLA-A*11:01-expressing individuals.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 570 ; 610
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Cross-Reactive Donor-Specific CD8+ Tregs Efficiently Prevent Transplant Rejection

    Elodie Picarda / Séverine Bézie / Lorena Usero / Jason Ossart / Marine Besnard / Hanim Halim / Klara Echasserieau / Claire Usal / Jamie Rossjohn / Karine Bernardeau / Stéphanie Gras / Carole Guillonneau

    Cell Reports, Vol 29, Iss 13, Pp 4245-4255.e

    2019  Volume 6

    Abstract: Summary: To reduce the use of non-specific immunosuppressive drugs detrimental to transplant patient health, therapies in development aim to achieve antigen-specific tolerance by promoting antigen-specific regulatory T cells (Tregs). However, ... ...

    Abstract Summary: To reduce the use of non-specific immunosuppressive drugs detrimental to transplant patient health, therapies in development aim to achieve antigen-specific tolerance by promoting antigen-specific regulatory T cells (Tregs). However, identification of the natural antigens recognized by Tregs and the contribution of their dominance in transplantation has been challenging. We identify epitopes derived from distinct major histocompatibility complex (MHC) class II molecules, sharing a 7-amino acid consensus sequence positioned in a central mobile section in complex with MHC class I, recognized by cross-reactive CD8+ Tregs, enriched in the graft. Antigen-specific CD8+ Tregs can be induced in vivo with a 16-amino acid-long peptide to trigger transplant tolerance. Peptides derived from human HLA class II molecules, harboring the rat consensus sequence, also activate and expand human CD8+ Tregs, suggesting its potential in human transplantation. Altogether, this work should facilitate the development of therapies with peptide epitopes for transplantation and improve our understanding of CD8+ Treg recognition. : Picarda et al. describe MHC class II-derived peptides recognized by cross-reactive CD8+ Tregs instrumental for tolerance induction in transplantation between an incompatible donor and recipient. Keywords: transplantation, tolerance, peptide, CD8+, rat, human, therapy, regulation, antigen-specific
    Keywords Biology (General) ; QH301-705.5
    Subject code 610
    Language English
    Publishing date 2019-12-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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