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  1. Article ; Online: Mechanism and evolution of human ACE2 binding by SARS-CoV-2 spike.

    Wrobel, Antoni G

    Current opinion in structural biology

    2023  Volume 81, Page(s) 102619

    Abstract: Spike glycoprotein of SARS-CoV-2 mediates viral entry into host cells by facilitating virus attachment and membrane fusion. ACE2 is the main receptor of SARS-CoV-2 and its interaction with spike has shaped the virus' emergence from an animal reservoir ... ...

    Abstract Spike glycoprotein of SARS-CoV-2 mediates viral entry into host cells by facilitating virus attachment and membrane fusion. ACE2 is the main receptor of SARS-CoV-2 and its interaction with spike has shaped the virus' emergence from an animal reservoir and subsequent evolution in the human host. Many structural studies on the spike:ACE2 interaction have provided insights into mechanisms driving viral evolution during the on-going pandemic. This review describes the molecular basis of spike binding to ACE2, outlines mechanisms that have optimised this interaction during viral evolution, and suggests directions for future research.
    MeSH term(s) Animals ; Humans ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Carrier Proteins/metabolism ; COVID-19 ; Protein Binding ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Carrier Proteins ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23)
    Language English
    Publishing date 2023-05-15
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2023.102619
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  2. Article ; Online: Hold your horses: The receptor-binding domains of SARS-CoV-2, SARS-CoV, and hCoV-NL63 bind equine ACE2.

    Nawrath, Philipp / Wrobel, Antoni G

    Structure (London, England : 1993)

    2022  Volume 30, Issue 10, Page(s) 1367–1368

    Abstract: In this issue of Structure, Lan and colleagues seek to identify regions on the ACE2 receptor and coronavirus spikes that are essential for the viral attachment. They achieve it through a detailed comparative analysis of the binding of coronaviruses NL63, ...

    Abstract In this issue of Structure, Lan and colleagues seek to identify regions on the ACE2 receptor and coronavirus spikes that are essential for the viral attachment. They achieve it through a detailed comparative analysis of the binding of coronaviruses NL63, SARS-CoV, and several SARS-CoV-2 variants with human and horse ACE2.
    MeSH term(s) Angiotensin-Converting Enzyme 2 ; Animals ; COVID-19 ; Coronavirus NL63, Human ; Horses ; Humans ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/metabolism ; SARS-CoV-2
    Chemical Substances Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2022-09-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2022.09.003
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  3. Article ; Online: Development of high affinity broadly reactive aptamers for spike protein of multiple SARS-CoV-2 variants.

    Le, Thao T / Benton, Donald J / Wrobel, Antoni G / Gamblin, Steven J

    RSC advances

    2023  Volume 13, Issue 22, Page(s) 15322–15326

    Abstract: We have developed broadly reactive aptamers against multiple variants by alternating the target between spike proteins from different SARS-CoV-2 variants during the selection process. In this process we have developed aptamers which can recognise all ... ...

    Abstract We have developed broadly reactive aptamers against multiple variants by alternating the target between spike proteins from different SARS-CoV-2 variants during the selection process. In this process we have developed aptamers which can recognise all variants, from the original wild-type 'Wuhan' strain to Omicron, with high affinity (
    Language English
    Publishing date 2023-05-19
    Publishing country England
    Document type Journal Article
    ISSN 2046-2069
    ISSN (online) 2046-2069
    DOI 10.1039/d3ra01382k
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  4. Article ; Online: Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel.

    Ng, Kevin W / Faulkner, Nikhil / Wrobel, Antoni G / Gamblin, Steve J / Kassiotis, George

    Seminars in immunology

    2021  Volume 55, Page(s) 101507

    Abstract: Coronaviruses are evolutionarily successful RNA viruses, common to multiple avian, amphibian and mammalian hosts. Despite their ubiquity and potential impact, knowledge of host immunity to coronaviruses remains incomplete, partly owing to the lack of ... ...

    Abstract Coronaviruses are evolutionarily successful RNA viruses, common to multiple avian, amphibian and mammalian hosts. Despite their ubiquity and potential impact, knowledge of host immunity to coronaviruses remains incomplete, partly owing to the lack of overt pathogenicity of endemic human coronaviruses (HCoVs), which typically cause common colds. However, the need for deeper understanding became pressing with the zoonotic introduction of three novel coronaviruses in the past two decades, causing severe acute respiratory syndromes in humans, and the unfolding pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). This renewed interest not only triggered the discovery of two of the four HCoVs, but also uncovered substantial cellular and humoral cross-reactivity with shared or related coronaviral antigens. Here, we review the evidence for cross-reactive B cell memory elicited by HCoVs and its potential impact on the puzzlingly variable outcome of SARS-CoV-2 infection. The available data indicate targeting of highly conserved regions primarily in the S2 subunits of the spike glycoproteins of HCoVs and SARS-CoV-2 by cross-reactive B cells and antibodies. Rare monoclonal antibodies reactive with conserved S2 epitopes and with potent virus neutralising activity have been cloned, underscoring the potential functional relevance of cross-reactivity. We discuss B cell and antibody cross-reactivity in the broader context of heterologous humoral immunity to coronaviruses, as well as the limits of protective immune memory against homologous re-infection. Given the bidirectional nature of cross-reactivity, the unprecedented current vaccination campaign against SARS-CoV-2 is expected to impact HCoVs, as well as future zoonotic coronaviruses attempting to cross the species barrier. However, emerging SARS-CoV-2 variants with resistance to neutralisation by vaccine-induced antibodies highlight a need for targeting more constrained, less mutable parts of the spike. The delineation of such cross-reactive areas, which humoral immunity can be trained to attack, may offer the key to permanently shifting the balance of our interaction with current and future coronaviruses in our favour.
    MeSH term(s) Animals ; Antibodies, Viral ; COVID-19 ; Humans ; Immunity, Humoral ; SARS-CoV-2
    Chemical Substances Antibodies, Viral
    Language English
    Publishing date 2021-10-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1018141-6
    ISSN 1096-3618 ; 1044-5323
    ISSN (online) 1096-3618
    ISSN 1044-5323
    DOI 10.1016/j.smim.2021.101507
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    Zs.A 2843: Show issues Location:
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  5. Article ; Online: Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein.

    Calvaresi, Valeria / Wrobel, Antoni G / Toporowska, Joanna / Hammerschmid, Dietmar / Doores, Katie J / Bradshaw, Richard T / Parsons, Ricardo B / Benton, Donald J / Roustan, Chloë / Reading, Eamonn / Malim, Michael H / Gamblin, Steve J / Politis, Argyris

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1421

    Abstract: SARS-CoV-2 spike glycoprotein mediates receptor binding and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displays more exposed antigenic ... ...

    Abstract SARS-CoV-2 spike glycoprotein mediates receptor binding and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displays more exposed antigenic surface. Spikes of variants of concern (VOCs) acquired amino acid changes linked to increased virulence and immune evasion. Here, using HDX-MS, we identified changes in spike dynamics that we associate with the transition from closed to open conformations, to ACE2 binding, and to specific mutations in VOCs. We show that the RBD-associated subdomain plays a role in spike opening, whereas the NTD acts as a hotspot of conformational divergence of VOC spikes driving immune evasion. Alpha, beta and delta spikes assume predominantly open conformations and ACE2 binding increases the dynamics of their core helices, priming spikes for fusion. Conversely, substitutions in omicron spike lead to predominantly closed conformations, presumably enabling it to escape antibodies. At the same time, its core helices show characteristics of being pre-primed for fusion even in the absence of ACE2. These data inform on SARS-CoV-2 evolution and omicron variant emergence.
    MeSH term(s) Humans ; Spike Glycoprotein, Coronavirus/genetics ; Angiotensin-Converting Enzyme 2 ; COVID-19 ; SARS-CoV-2/genetics ; Mutation
    Chemical Substances spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2023-03-14
    Publishing country England
    Document type Journal Article ; 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/s41467-023-36745-0
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  6. Article ; Online: Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.

    Olajide, Okikiola M / Osman, Maria Kaukab / Robert, Jonathan / Kessler, Susanne / Toews, Lina Kathrin / Thamamongood, Thiprampai / Neefjes, Jacques / Wrobel, Antoni G / Schwemmle, Martin / Ciminski, Kevin / Reuther, Peter

    PLoS biology

    2023  Volume 21, Issue 7, Page(s) e3002182

    Abstract: The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II ...

    Abstract The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II (MHC-II) for cell entry. MHC-II proteins from various vertebrate species can facilitate infection with the bat IAV H18N11. Yet, it has been difficult to biochemically determine the H18:MHC-II binding. Here, we followed a different approach and generated MHC-II chimeras from the human leukocyte antigen DR (HLA-DR), which supports H18-mediated entry, and the nonclassical MHC-II molecule HLA-DM, which does not. In this context, viral entry was supported only by a chimera containing the HLA-DR α1, α2, and β1 domains. Subsequent modeling of the H18:HLA-DR interaction identified the α2 domain as central for this interaction. Further mutational analyses revealed highly conserved amino acids within loop 4 (N149) and β-sheet 6 (V190) of the α2 domain as critical for virus entry. This suggests that conserved residues in the α1, α2, and β1 domains of MHC-II mediate H18-binding and virus propagation. The conservation of MHC-II amino acids, which are critical for H18N11 binding, may explain the broad species specificity of this virus.
    MeSH term(s) Animals ; Humans ; Influenza A virus ; Chiroptera ; Amino Acids ; Histocompatibility Antigens Class II ; HLA-DR Antigens/metabolism ; HLA Antigens
    Chemical Substances Amino Acids ; Histocompatibility Antigens Class II ; HLA-DR Antigens ; HLA Antigens
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3002182
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    Zs.A 6193: Show issues Location:
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  7. Article ; Online: Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.

    Okikiola M Olajide / Maria Kaukab Osman / Jonathan Robert / Susanne Kessler / Lina Kathrin Toews / Thiprampai Thamamongood / Jacques Neefjes / Antoni G Wrobel / Martin Schwemmle / Kevin Ciminski / Peter Reuther

    PLoS Biology, Vol 21, Iss 7, p e

    2023  Volume 3002182

    Abstract: The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II ...

    Abstract The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II (MHC-II) for cell entry. MHC-II proteins from various vertebrate species can facilitate infection with the bat IAV H18N11. Yet, it has been difficult to biochemically determine the H18:MHC-II binding. Here, we followed a different approach and generated MHC-II chimeras from the human leukocyte antigen DR (HLA-DR), which supports H18-mediated entry, and the nonclassical MHC-II molecule HLA-DM, which does not. In this context, viral entry was supported only by a chimera containing the HLA-DR α1, α2, and β1 domains. Subsequent modeling of the H18:HLA-DR interaction identified the α2 domain as central for this interaction. Further mutational analyses revealed highly conserved amino acids within loop 4 (N149) and β-sheet 6 (V190) of the α2 domain as critical for virus entry. This suggests that conserved residues in the α1, α2, and β1 domains of MHC-II mediate H18-binding and virus propagation. The conservation of MHC-II amino acids, which are critical for H18N11 binding, may explain the broad species specificity of this virus.
    Keywords Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Author Correction: SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.

    Wrobel, Antoni G / Benton, Donald J / Xu, Pengqi / Roustan, Chloë / Martin, Stephen R / Rosenthal, Peter B / Skehel, John J / Gamblin, Steven J

    Nature structural & molecular biology

    2020  Volume 27, Issue 10, Page(s) 1001

    Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

    Abstract An amendment to this paper has been published and can be accessed via a link at the top of the paper.
    Keywords covid19
    Language English
    Publishing date 2020-08-14
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-020-0509-2
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  9. Article ; Online: Evolution of the SARS-CoV-2 spike protein in the human host

    Antoni G. Wrobel / Donald J. Benton / Chloë Roustan / Annabel Borg / Saira Hussain / Stephen R. Martin / Peter B. Rosenthal / John J. Skehel / Steven J. Gamblin

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

    2022  Volume 7

    Abstract: The SARS-CoV-2 spike has been evolving in the human population. The variants of concern alpha and beta evolved to optimise spike openness and so ability to bind its receptor ACE2, the affinity towards the receptor, and stability upon receptor binding. ...

    Abstract The SARS-CoV-2 spike has been evolving in the human population. The variants of concern alpha and beta evolved to optimise spike openness and so ability to bind its receptor ACE2, the affinity towards the receptor, and stability upon receptor binding.
    Keywords Science ; Q
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
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  10. Article ; Online: Evolution of the SARS-CoV-2 spike protein in the human host.

    Wrobel, Antoni G / Benton, Donald J / Roustan, Chloë / Borg, Annabel / Hussain, Saira / Martin, Stephen R / Rosenthal, Peter B / Skehel, John J / Gamblin, Steven J

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 1178

    Abstract: Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have examined the structure and receptor binding properties ... ...

    Abstract Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have examined the structure and receptor binding properties of spike proteins from the B.1.1.7 (Alpha) and B.1.351 (Beta) variants to better understand the evolution of the virus in humans. Spikes of both variants have the same mutation, N501Y, in the receptor-binding domains. This substitution confers tighter ACE2 binding, dependent on the common earlier substitution, D614G. Each variant spike has acquired other key changes in structure that likely impact virus pathogenesis. The spike from the Alpha variant is more stable against disruption upon binding ACE2 receptor than all other spikes studied. This feature is linked to the acquisition of a more basic substitution at the S1-S2 furin site (also observed for the variants of concern Delta, Kappa, and Omicron) which allows for near-complete cleavage. In the Beta variant spike, the presence of a new substitution, K417N (also observed in the Omicron variant), in combination with the D614G, stabilises a more open spike trimer, a conformation required for receptor binding. Our observations suggest ways these viruses have evolved to achieve greater transmissibility in humans.
    MeSH term(s) Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Angiotensin-Converting Enzyme 2/ultrastructure ; Binding Sites/genetics ; COVID-19/metabolism ; COVID-19/transmission ; COVID-19/virology ; Cryoelectron Microscopy ; Cytopathogenic Effect, Viral/genetics ; Evolution, Molecular ; Host-Pathogen Interactions ; Humans ; Kinetics ; Models, Molecular ; Mutation, Missense ; Protein Binding ; Protein Domains ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2022-03-04
    Publishing country England
    Document type Journal Article ; 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/s41467-022-28768-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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