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  1. Article: Structural Basis for Accommodation of Emerging B.1.351 and B.1.1.7 Variants by Two Potent SARS-CoV-2 Neutralizing Antibodies.

    Cerutti, Gabriele / Rapp, Micah / Guo, Yicheng / Bahna, Fabiana / Bimela, Jude / Reddem, Eswar R / Yu, Jian / Wang, Pengfei / Liu, Lihong / Huang, Yaoxing / Ho, David D / Kwong, Peter D / Sheng, Zizhang / Shapiro, Lawrence

    bioRxiv : the preprint server for biology

    2021  

    Abstract: Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively show ... binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies like 1-57 and 2-7 ... antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of spike, was unaffected ...

    Abstract Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of spike, was unaffected by these emerging strains. Here, we report cryo-EM structures of 1-57 and 2-7 in complex with spike, revealing each of these antibodies to utilize a distinct mechanism to bypass or accommodate RBD mutations. Notably, each antibody represented a response with recognition distinct from those of frequent antibody classes. Moreover, many epitope residues recognized by 1-57 and 2-7 were outside hotspots of evolutionary pressure for both ACE2 binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies like 1-57 and 2-7, which target less prevalent epitopes, could ameliorate issues of monoclonal antibody escape.
    Language English
    Publishing date 2021-02-22
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2021.02.21.432168
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies.

    Cerutti, Gabriele / Rapp, Micah / Guo, Yicheng / Bahna, Fabiana / Bimela, Jude / Reddem, Eswar R / Yu, Jian / Wang, Pengfei / Liu, Lihong / Huang, Yaoxing / Ho, David D / Kwong, Peter D / Sheng, Zizhang / Shapiro, Lawrence

    Structure (London, England : 1993)

    2021  Volume 29, Issue 7, Page(s) 655–663.e4

    Abstract: Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively, show ... binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies, such as 1-57 and 2 ... antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of the spike, was unaffected ...

    Abstract Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively, show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of the spike, was unaffected by these emerging strains. Here, we report cryo-EM structures of 1-57 and 2-7 in complex with spike, revealing each of these antibodies to utilize a distinct mechanism to bypass or accommodate RBD mutations. Notably, each antibody represented an immune response with recognition distinct from those of frequent antibody classes. Moreover, many epitope residues recognized by 1-57 and 2-7 were outside hotspots of evolutionary pressure for ACE2 binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies, such as 1-57 and 2-7, which target less prevalent epitopes, could ameliorate issues of monoclonal antibody escape.
    MeSH term(s) Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/immunology ; Angiotensin-Converting Enzyme 2/metabolism ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/genetics ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/chemistry ; Antibodies, Viral/genetics ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Binding Sites ; Cloning, Molecular ; Cryoelectron Microscopy ; Epitopes/chemistry ; Epitopes/genetics ; Epitopes/immunology ; Epitopes/metabolism ; Gene Expression ; HEK293 Cells ; Humans ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Receptors, Virus/chemistry ; Receptors, Virus/genetics ; Receptors, Virus/immunology ; Receptors, Virus/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Recombinant Proteins/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Receptors, Virus ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2021-06-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2021.05.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Structural Basis for Accommodation of Emerging B.1.351 and B.1.1.7 Variants by Two Potent SARS-CoV-2 Neutralizing Antibodies

    Cerutti, Gabriele / Rapp, Micah / Guo, Yicheng / Bahna, Fabiana / Bimela, Jude / Reddem, Eswar R / Yu, Jian / Wang, Pengfei / Liu, Lihong / Huang, Yaoxing / Ho, David D / Kwong, Peter D / Sheng, Zizhang / Shapiro, Lawrence

    bioRxiv

    Abstract: Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively show ... binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies like 1-57 and 2-7 ... antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of spike, was unaffected ...

    Abstract Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of spike, was unaffected by these emerging strains. Here, we report cryo-EM structures of 1-57 and 2-7 in complex with spike, revealing each of these antibodies to utilize a distinct mechanism to bypass or accommodate RBD mutations. Notably, each antibody represented a response with recognition distinct from those of frequent antibody classes. Moreover, many epitope residues recognized by 1-57 and 2-7 were outside hotspots of evolutionary pressure for both ACE2 binding and neutralizing antibody escape. We suggest the therapeutic use of antibodies like 1-57 and 2-7, which target less prevalent epitopes, could ameliorate issues of monoclonal antibody escape.
    Keywords covid19
    Language English
    Publishing date 2021-02-22
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2021.02.21.432168
    Database COVID19

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    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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