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  1. Article ; Online: A structural view of the SARS-CoV-2 virus and its assembly.

    Hardenbrook, Nathan J / Zhang, Peijun

    Current opinion in virology

    2021  Volume 52, Page(s) 123–134

    Abstract: The SARS-CoV-2 pandemic that struck in 2019 has left the world crippled with hundreds of millions of cases and millions of people dead. During this time, we have seen unprecedented support and collaboration amongst scientists to respond to this deadly ... ...

    Abstract The SARS-CoV-2 pandemic that struck in 2019 has left the world crippled with hundreds of millions of cases and millions of people dead. During this time, we have seen unprecedented support and collaboration amongst scientists to respond to this deadly disease. Advances in the field of structural biology, in particular cryoEM and cryo-electron tomography, have allowed unprecedented structural analysis of SARS-CoV-2. Here, we review the structural work on the SARS-CoV-2 virus and viral components, as well as its cellular assembly process, highlighting some important structural findings that have made significant impact on the protection from and treatment of emerging viral infections.
    MeSH term(s) COVID-19 ; Cryoelectron Microscopy ; Electron Microscope Tomography ; Humans ; Pandemics ; SARS-CoV-2
    Language English
    Publishing date 2021-12-04
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2611378-8
    ISSN 1879-6265 ; 1879-6257
    ISSN (online) 1879-6265
    ISSN 1879-6257
    DOI 10.1016/j.coviro.2021.11.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.

    Zhou, Kang / Liu, Shiheng / Hardenbrook, Nathan J / Cui, Yanxiang / Krantz, Bryan A / Zhou, Z Hong

    Structure (London, England : 1993)

    2020  Volume 28, Issue 8, Page(s) 879–887.e3

    Abstract: Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer ( ... ...

    Abstract Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA
    MeSH term(s) Antigens, Bacterial/chemistry ; Antigens, Bacterial/metabolism ; Bacterial Toxins/chemistry ; Bacterial Toxins/metabolism ; Cryoelectron Microscopy ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Multimerization
    Chemical Substances Antigens, Bacterial ; Bacterial Toxins ; anthrax toxin
    Language English
    Publishing date 2020-06-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2020.05.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.

    Hardenbrook, Nathan J / Liu, Shiheng / Zhou, Kang / Ghosal, Koyel / Zhou, Z Hong / Krantz, Bryan A

    Nature communications

    2020  Volume 11, Issue 1, Page(s) 840

    Abstract: Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels ... ...

    Abstract Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
    MeSH term(s) Amino Acid Sequence ; Antigens, Bacterial/chemistry ; Antigens, Bacterial/genetics ; Bacillus anthracis/genetics ; Bacillus anthracis/metabolism ; Bacterial Toxins/chemistry ; Bacterial Toxins/genetics ; Binding Sites ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Unfolding
    Chemical Substances Antigens, Bacterial ; Bacterial Toxins ; anthrax toxin
    Language English
    Publishing date 2020-02-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-020-14658-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors

    Nathan J. Hardenbrook / Shiheng Liu / Kang Zhou / Koyel Ghosal / Z. Hong Zhou / Bryan A. Krantz

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: Abstract Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA ... ...

    Abstract Abstract Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
    Keywords Science ; Q
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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