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  1. Article: Small Hero with Great Powers: Vaccinia Virus E3 Protein and Evasion of the Type I IFN Response.

    Szczerba, Mateusz / Subramanian, Sambhavi / Trainor, Kelly / McCaughan, Megan / Kibler, Karen V / Jacobs, Bertram L

    Biomedicines

    2022  Volume 10, Issue 2

    Abstract: Poxviridae have developed a plethora of strategies to evade innate and adaptive immunity. In this review, we focused on the vaccinia virus E3 protein, encoded by ... ...

    Abstract Poxviridae have developed a plethora of strategies to evade innate and adaptive immunity. In this review, we focused on the vaccinia virus E3 protein, encoded by the
    Language English
    Publishing date 2022-01-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines10020235
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Resistance analysis following sotrovimab treatment in participants with COVID-19 during the phase III COMET-ICE study.

    Subramanian, Sambhavi / Schnell, Gretja / Iulio, Julia di / Gupta, Anil K / Shapiro, Adrienne E / Sarkis, Elias H / Lopuski, Amanda / Peppercorn, Amanda / Aldinger, Melissa / Hebner, Christy M / Cathcart, Andrea L

    Future virology

    2023  

    Abstract: Aim: ...

    Abstract Aim:
    Language English
    Publishing date 2023-12-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 2254606-6
    ISSN 1746-0808 ; 1746-0794
    ISSN (online) 1746-0808
    ISSN 1746-0794
    DOI 10.2217/fvl-2023-0146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variants.

    Addetia, Amin / Piccoli, Luca / Case, James Brett / Park, Young-Jun / Beltramello, Martina / Guarino, Barbara / Dang, Ha / Pinto, Dora / Scheaffer, Suzanne / Sprouse, Kaitlin / Bassi, Jessica / Silacci-Fregni, Chiara / Muoio, Francesco / Dini, Marco / Vincenzetti, Lucia / Acosta, Rima / Johnson, Daisy / Subramanian, Sambhavi / Saliba, Christian /
    Giurdanella, Martina / Lombardo, Gloria / Leoni, Giada / Culap, Katja / McAlister, Carley / Rajesh, Anushka / Dellota, Exequiel / Zhou, Jiayi / Farhat, Nisar / Bohan, Dana / Noack, Julia / Lempp, Florian A / Cameroni, Elisabetta / Whitener, Bradley / Giannini, Olivier / Ceschi, Alessandro / Ferrari, Paolo / Franzetti-Pellanda, Alessandra / Biggiogero, Maira / Garzoni, Christian / Zappi, Stephanie / Bernasconi, Luca / Kim, Min Jeong / Schnell, Gretja / Czudnochowski, Nadine / Franko, Nicholas / Logue, Jennifer K / Yoshiyama, Courtney / Stewart, Cameron / Chu, Helen / Schmid, Michael A / Purcell, LIsa A / Snell, Gyorgy / Lanzavecchia, Antonio / Diamond, Michael / Corti, Davide / Veesler, David

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Currently circulating SARS-CoV-2 variants acquired convergent mutations at receptor-binding domain (RBD) hot spots. Their impact on viral infection, transmission, and efficacy of vaccines and therapeutics remains poorly understood. Here, we demonstrate ... ...

    Abstract Currently circulating SARS-CoV-2 variants acquired convergent mutations at receptor-binding domain (RBD) hot spots. Their impact on viral infection, transmission, and efficacy of vaccines and therapeutics remains poorly understood. Here, we demonstrate that recently emerged BQ.1.1. and XBB.1 variants bind ACE2 with high affinity and promote membrane fusion more efficiently than earlier Omicron variants. Structures of the BQ.1.1 and XBB.1 RBDs bound to human ACE2 and S309 Fab (sotrovimab parent) explain the altered ACE2 recognition and preserved antibody binding through conformational selection. We show that sotrovimab binds avidly to all Omicron variants, promotes Fc-dependent effector functions and protects mice challenged with BQ.1.1, the variant displaying the greatest loss of neutralization. Moreover, in several donors vaccine-elicited plasma antibodies cross-react with and trigger effector functions against Omicron variants despite reduced neutralizing activity. Cross-reactive RBD-directed human memory B cells remained dominant even after two exposures to Omicron spikes, underscoring persistent immune imprinting. Our findings suggest that this previously overlooked class of cross-reactive antibodies, exemplified by S309, may contribute to protection against disease caused by emerging variants through elicitation of effector functions.
    Language English
    Publishing date 2023-02-27
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.01.17.523798
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Neutralization, effector function and immune imprinting of Omicron variants.

    Addetia, Amin / Piccoli, Luca / Case, James Brett / Park, Young-Jun / Beltramello, Martina / Guarino, Barbara / Dang, Ha / de Melo, Guilherme Dias / Pinto, Dora / Sprouse, Kaitlin / Scheaffer, Suzanne M / Bassi, Jessica / Silacci-Fregni, Chiara / Muoio, Francesco / Dini, Marco / Vincenzetti, Lucia / Acosta, Rima / Johnson, Daisy / Subramanian, Sambhavi /
    Saliba, Christian / Giurdanella, Martina / Lombardo, Gloria / Leoni, Giada / Culap, Katja / McAlister, Carley / Rajesh, Anushka / Dellota, Exequiel / Zhou, Jiayi / Farhat, Nisar / Bohan, Dana / Noack, Julia / Chen, Alex / Lempp, Florian A / Quispe, Joel / Kergoat, Lauriane / Larrous, Florence / Cameroni, Elisabetta / Whitener, Bradley / Giannini, Olivier / Cippà, Pietro / Ceschi, Alessandro / Ferrari, Paolo / Franzetti-Pellanda, Alessandra / Biggiogero, Maira / Garzoni, Christian / Zappi, Stephanie / Bernasconi, Luca / Kim, Min Jeong / Rosen, Laura E / Schnell, Gretja / Czudnochowski, Nadine / Benigni, Fabio / Franko, Nicholas / Logue, Jennifer K / Yoshiyama, Courtney / Stewart, Cameron / Chu, Helen / Bourhy, Hervé / Schmid, Michael A / Purcell, Lisa A / Snell, Gyorgy / Lanzavecchia, Antonio / Diamond, Michael S / Corti, Davide / Veesler, David

    Nature

    2023  Volume 621, Issue 7979, Page(s) 592–601

    Abstract: Currently circulating SARS-CoV-2 variants have acquired convergent mutations at hot spots in the receptor-binding ... ...

    Abstract Currently circulating SARS-CoV-2 variants have acquired convergent mutations at hot spots in the receptor-binding domain
    MeSH term(s) Animals ; Cricetinae ; Humans ; Mice ; Angiotensin-Converting Enzyme 2/immunology ; Angiotensin-Converting Enzyme 2/metabolism ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/immunology ; COVID-19/immunology ; COVID-19/prevention & control ; COVID-19/virology ; Cross Reactions ; Immune Evasion ; Membrane Fusion ; Neutralization Tests ; SARS-CoV-2/classification ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; Mutation ; Memory B Cells/immunology ; COVID-19 Vaccines/immunology
    Chemical Substances ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; S309 antibody ; sotrovimab (1MTK0BPN8V) ; spike protein, SARS-CoV-2 ; COVID-19 Vaccines
    Language English
    Publishing date 2023-08-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06487-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 26: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  5. Article ; Online: Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variants

    Addetia, Amin / Piccoli, Luca / Case, James Brett / Park, Young-Jun / Beltramello, Martina / Guarino, Barbara / Dang, Ha / Pinto, Dora / Scheaffer, Suzanne / Sprouse, Kaitlin / Bassi, Jessica / Silacci-Fregni, Chiara / Muoio, Francesco / Dini, Marco / Vincenzetti, Lucia / Acosta, Rima / Johnson, Daisy / Subramanian, Sambhavi / Saliba, Christian /
    Giurdanella, Martina / Lombardo, Gloria / Leoni, Giada / Culap, Katja / McAlister, Carley / Rajesh, Anushka / Dellota, Exequiel / Cameroni, Elisabetta / Whitener, Bradley / Giannini, Olivier / Ceschi, Alessandro / Ferrari, Paolo / Franzetti-Pellanda, Alessandra / Biggiogero, Maira / Garzoni, Christian / Zappi, Stephanie / Bernasconi, Luca / Kim, Min Jeong / Schnell, Gretja / Czudnochowski, Nadine / Franko, Nicholas / Logue, Jennifer K. / Yoshiyama, Courtney / Stewart, Cameron / Chu, Helen / Schmid, Michael A. / Purcell, LIsa A. / Snell, Gyorgy / Lanzavecchia, Antonio / Diamond, Michael / Corti, Davide / Veesler, David

    bioRxiv

    Abstract: Currently circulating SARS-CoV-2 variants acquired convergent mutations at receptor-binding domain (RBD) hot spots. Their impact on viral infection, transmission, and efficacy of vaccines and therapeutics remains poorly understood. Here, we demonstrate ... ...

    Abstract Currently circulating SARS-CoV-2 variants acquired convergent mutations at receptor-binding domain (RBD) hot spots. Their impact on viral infection, transmission, and efficacy of vaccines and therapeutics remains poorly understood. Here, we demonstrate that recently emerged BQ.1.1. and XBB.1 variants bind ACE2 with high affinity and promote membrane fusion more efficiently than earlier Omicron variants. Structures of the BQ.1.1 and XBB.1 RBDs bound to human ACE2 and S309 Fab (sotrovimab parent) explain the altered ACE2 recognition and preserved antibody binding through conformational selection. We show that sotrovimab binds avidly to all Omicron variants, promotes Fc-dependent effector functions and protects mice challenged with BQ.1.1, the variant displaying the greatest loss of neutralization. Moreover, in several donors vaccine-elicited plasma antibodies cross-react with and trigger effector functions against Omicron variants despite reduced neutralizing activity. Cross-reactive RBD-directed human memory B cells remained dominant even after two exposures to Omicron spikes, underscoring persistent immune imprinting. Our findings suggest that this previously overlooked class of cross-reactive antibodies, exemplified by S309, may contribute to protection against disease caused by emerging variants through elicitation of effector functions.
    Keywords covid19
    Language English
    Publishing date 2023-01-17
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2023.01.17.523798
    Database COVID19

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  6. Article ; Online: The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2

    Cathcart, Andrea L / Havenar-Daughton, Colin / Lempp, Florian A / Ma, Daphne / Schmid, Michael / Agostini, Maria L / Guarino, Barbara / Di iulio, Julia / Rosen, Laura / Tucker, Heather / Dillen, Joshua / Subramanian, Sambhavi / Sloan, Barbara / Bianchi, Siro / Wojcechowskyj, Jason / Zhou, Jiayi / Kaiser, Hannah / Chase, Arthur / Montiel-Ruiz, Martin /
    Czudnochowski, Nadine / Cameroni, Elisabetta / Ledoux, Sarah / Colas, Christophe / Soriaga, Leah / Telenti, Amalio / Hwang, Seungmin / Snell, Gyorgy / Virgin, Herbert W / Corti, Davide / Hebner, Christy M

    bioRxiv

    Abstract: VIR-7831 and VIR-7832 are dual action monoclonal antibodies (mAbs) targeting the spike glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). VIR-7831 and VIR-7832 were derived from a parent antibody (S309) isolated from memory B ... ...

    Abstract VIR-7831 and VIR-7832 are dual action monoclonal antibodies (mAbs) targeting the spike glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). VIR-7831 and VIR-7832 were derived from a parent antibody (S309) isolated from memory B cells of a 2003 severe acute respiratory syndrome coronavirus (SARS-CoV) survivor. Both mAbs contain an LS mutation in the Fc region to prolong serum half-life and potentially enhance distribution to the respiratory mucosa. In addition, VIR-7832 encodes an Fc GAALIE mutation that has been shown previously to evoke CD8+ T-cells in the context of an in vivo viral respiratory infection. VIR-7831 and VIR-7832 potently neutralize live wild-type SARS-CoV-2 in vitro as well as pseudotyped viruses encoding spike protein from the B.1.1.7, B.1.351 and P.1 variants. In addition, they retain activity against monoclonal antibody resistance mutations that confer reduced susceptibility to currently authorized mAbs. The VIR-7831/VIR-7832 epitope does not overlap with mutational sites in the current variants of concern and continues to be highly conserved among circulating sequences consistent with the high barrier to resistance observed in vitro. Furthermore, both mAbs can recruit effector mechanisms in vitro that may contribute to clinical efficacy via elimination of infected host cells. In vitro studies with these mAbs demonstrated no enhancement of infection. In a Syrian Golden hamster proof-of concept concept wildtype SARS-CoV-2 infection model, animals treated with VIR-7831 had less weight loss, and significantly decreased total viral load and infectious virus levels in the lung compared to a control mAb. Taken together, these data indicate that VIR-7831 and VIR-7832 are promising new agents in the fight against COVID-19.
    Keywords covid19
    Language English
    Publishing date 2021-03-10
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2021.03.09.434607
    Database COVID19

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