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  1. Article ; Online: SARS-CoV-2 neutralising antibodies after a second BA.5 bivalent booster.

    Wang, Qian / Bowen, Anthony / Ho, Jerren / Zhang, Richard M / Valdez, Riccardo / Stoneman, Emily / Gordon, Aubree / Liu, Lihong / Ho, David D

    Lancet (London, England)

    2023  Volume 402, Issue 10415, Page(s) 1827–1828

    MeSH term(s) Humans ; SARS-CoV-2 ; COVID-19 ; Antibodies, Neutralizing ; Antibodies, Viral
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral
    Language English
    Publishing date 2023-10-31
    Publishing country England
    Document type Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3306-6
    ISSN 1474-547X ; 0023-7507 ; 0140-6736
    ISSN (online) 1474-547X
    ISSN 0023-7507 ; 0140-6736
    DOI 10.1016/S0140-6736(23)02278-X
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ua VI Zs.5: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 94: Show issues

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  2. Article ; Online: Antibody neutralisation of emerging SARS-CoV-2 subvariants: EG.5.1 and XBC.1.6.

    Wang, Qian / Guo, Yicheng / Zhang, Richard M / Ho, Jerren / Mohri, Hiroshi / Valdez, Riccardo / Manthei, David M / Gordon, Aubree / Liu, Lihong / Ho, David D

    The Lancet. Infectious diseases

    2023  Volume 23, Issue 10, Page(s) e397–e398

    MeSH term(s) Humans ; SARS-CoV-2 ; COVID-19 ; Immunoglobulins ; Antibodies, Viral ; Antibodies, Neutralizing/therapeutic use
    Chemical Substances Immunoglobulins ; Antibodies, Viral ; Antibodies, Neutralizing
    Language English
    Publishing date 2023-09-11
    Publishing country United States
    Document type Letter
    ZDB-ID 2061641-7
    ISSN 1474-4457 ; 1473-3099
    ISSN (online) 1474-4457
    ISSN 1473-3099
    DOI 10.1016/S1473-3099(23)00555-8
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5743: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike.

    Wang, Qian / Guo, Yicheng / Liu, Liyuan / Schwanz, Logan T / Li, Zhiteng / Nair, Manoj S / Ho, Jerren / Zhang, Richard M / Iketani, Sho / Yu, Jian / Huang, Yiming / Qu, Yiming / Valdez, Riccardo / Lauring, Adam S / Huang, Yaoxing / Gordon, Aubree / Wang, Harris H / Liu, Lihong / Ho, David D

    Nature

    2023  Volume 624, Issue 7992, Page(s) 639–644

    Abstract: A severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron subvariant, BA.2.86, has emerged and spread to numerous countries worldwide, raising alarm because its spike protein contains 34 additional mutations compared with its BA.2 ... ...

    Abstract A severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron subvariant, BA.2.86, has emerged and spread to numerous countries worldwide, raising alarm because its spike protein contains 34 additional mutations compared with its BA.2 predecessor
    MeSH term(s) Humans ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; COVID-19/immunology ; COVID-19/virology ; COVID-19 Vaccines/immunology ; Epitopes, B-Lymphocyte/immunology ; Immunogenicity, Vaccine ; Mutation ; Receptors, Virus/metabolism ; SARS-CoV-2/classification ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Immune Sera/immunology
    Chemical Substances Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Epitopes, B-Lymphocyte ; Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Immune Sera
    Language English
    Publishing date 2023-10-23
    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/s41586-023-06750-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    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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  4. Article ; Online: Antibody Neutralization of Emerging SARS-CoV-2: EG.5.1 and XBC.1.6

    Wang, Qian / Guo, Yicheng / Zhang, Richard M. / Ho, Jerren / Mohri, Hiroshi / Valdez, Riccardo / Manthei, David M. / Gordon, Aubree / Liu, Lihong / Ho, David D.

    bioRxiv

    Abstract: SARS-CoV-2 variants EG.5.1 and XBC.1.6 have recently emerged, attracting increased attention due to their rapid expansion globally and in Australia, respectively. EG.5.1 evolved from Omicron subvariant XBB.1.9, harboring additional Q52H and F456L spike ... ...

    Abstract SARS-CoV-2 variants EG.5.1 and XBC.1.6 have recently emerged, attracting increased attention due to their rapid expansion globally and in Australia, respectively. EG.5.1 evolved from Omicron subvariant XBB.1.9, harboring additional Q52H and F456L spike substitutions. The F456L mutation is located within the epitopes of many class-1 monoclonal antibodies (mAbs) directed to the receptor-binding domain (RBD), raising concerns about further antibody evasion. XBC.1.6, a descendant of a Delta-BA.2 recombinant, carries 15 additional spike mutations. The extent to which antibody evasion contributes to the growth advantage of XBC.1.6 in Australia remains to be determined. To assess the antibody evasion properties of the emergent variants, we conducted pseudovirus neutralization assays using sera from individuals who received three doses of COVID-19 mRNA monovalent vaccines plus one dose of a BA.5 bivalent vaccine, as well as from patients with BQ or XBB breakthrough infection. The assays were also performed using a panel of 14 mAbs that retained neutralizing activity against prior XBB subvariants. Our data suggested that EG.5.1 was slightly but significantly more resistant (< 2-fold) to neutralization by BQ and XBB breakthrough sera than XBB.1.16, which is known to be antigenically similar to XBB.1.5. Moreover, the F456L mutation in EG.5.1 conferred heightened resistance to certain RBD class-1 mAbs. In contrast, XBC.1.6 was more sensitive to neutralization by sera and mAbs than the XBB subvariants. Notably, XBB breakthrough sera retained only weak neutralization activity against XBB subvariants. In summary, EG.5.1 and XBC.1.6 exhibited distinct antibody evasion properties. The recent global expansion of EG.5.1 might be attributable, in part, to its enhanced neutralization resistance. That XBB breakthrough infections did not elicit a robust antibody neutralization response against XBB subvariants is indicative of immunological imprinting. The high prevalence of XBC.1.6 in Australia is not due to enhanced antibody evasion.
    Keywords covid19
    Language English
    Publishing date 2023-08-22
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2023.08.21.553968
    Database COVID19

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  5. Article ; Online: Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike

    Wang, Qian / Guo, Yicheng / Liu, Liyuan / Schwanz, Logan T / Li, Zhiteng / Ho, Jerren / Zhang, Richard M / Iketani, Sho / Yu, Jian / Huang, Yiming / Qu, Yiming / Valdez, Riccardo / Lauring, Adam S / Gordon, Aubree / Wang, Harris H / Liu, Lihong / Ho, David D

    bioRxiv

    Abstract: Although the COVID-19 pandemic has officially ended, SARS-CoV-2 continues to spread and evolve. Recent infections have been dominated by XBB.1.5 and EG.5.1 subvariants. A new subvariant designated BA.2.86 has just emerged, spreading to 21 countries in 5 ... ...

    Abstract Although the COVID-19 pandemic has officially ended, SARS-CoV-2 continues to spread and evolve. Recent infections have been dominated by XBB.1.5 and EG.5.1 subvariants. A new subvariant designated BA.2.86 has just emerged, spreading to 21 countries in 5 continents. This virus contains 34 spike mutations compared to its BA.2 predecessor, thereby raising concerns about its propensity to evade existing antibodies. We examined its antigenicity using human sera and monoclonal antibodies (mAbs). Reassuringly, BA.2.86 was not more resistant to human sera than XBB.1.5 and EG.5.1, indicating that the new subvariant would not have a growth advantage in this regard. Importantly, sera from patients who had XBB breakthrough infection exhibited robust neutralizing activity against all viruses tested, suggesting that upcoming XBB.1.5 monovalent vaccines could confer added protection. The finding that the longer genetic distance of BA.2.86 did not yield a larger antigenic distance was partially explained by the mAb data. While BA.2.86 showed greater resistance to mAbs to subdomain 1 (SD1) and receptor-binding domain (RBD) class 2 and 3 epitopes, it was more sensitive to mAbs to class 1 and 4/1 epitopes in the inner face of RBD that is exposed only when this domain is in the up position. We also identified six new spike mutations that mediate antibody resistance, including E554K that threatens SD1 mAbs in clinical development. The BA.2.86 spike also had a remarkably high receptor affinity. The ultimate trajectory of this new SARS-CoV-2 variant will soon be revealed by continuing surveillance, but its worldwide spread is worrisome.
    Keywords covid19
    Language English
    Publishing date 2023-09-25
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2023.09.24.559214
    Database COVID19

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