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  1. Artikel ; Online: TMPRSS2 est le récepteur cellulaire du coronavirus saisonnier HKU1.

    Saunders, Nell / Schwartz, Olivier

    Medecine sciences : M/S

    2024  Band 40, Heft 4, Seite(n) 335–337

    Titelübersetzung TMPRSS2 is the receptor of seasonal coronavirus HKU1.
    Mesh-Begriff(e) Humans ; Serine Endopeptidases/metabolism ; Serine Endopeptidases/physiology ; Serine Endopeptidases/genetics ; Seasons ; Receptors, Virus/physiology ; Receptors, Virus/metabolism ; Animals ; COVID-19 ; Coronavirus/physiology ; SARS-CoV-2/physiology
    Chemische Substanzen TMPRSS2 protein, human (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Receptors, Virus
    Sprache Französisch
    Erscheinungsdatum 2024-04-23
    Erscheinungsland France
    Dokumenttyp News ; Journal Article
    ZDB-ID 632733-3
    ISSN 1958-5381 ; 0767-0974
    ISSN (online) 1958-5381
    ISSN 0767-0974
    DOI 10.1051/medsci/2024034
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Dynamic label-free analysis of SARS-CoV-2 infection reveals virus-induced subcellular remodeling.

    Saunders, Nell / Monel, Blandine / Cayet, Nadege / Archetti, Lorenzo / Moreno, Hugo / Jeanne, Alexandre / Marguier, Agathe / Wai, Timothy / Schwartz, Olivier / Frechin, Mathieu

    bioRxiv

    Abstract: Assessing the impact of SARS-CoV-2 on organelle dynamics allows a better understanding of the mechanisms of viral replication. We combine label-free holo-tomographic microscopy (HTM) with Artificial Intelligence (AI) to visualize and quantify the ... ...

    Abstract Assessing the impact of SARS-CoV-2 on organelle dynamics allows a better understanding of the mechanisms of viral replication. We combine label-free holo-tomographic microscopy (HTM) with Artificial Intelligence (AI) to visualize and quantify the subcellular changes triggered by SARS-CoV-2 infection. We study the dynamics of shape, position and dry mass of nucleoli, nuclei, lipid droplets (LD) and mitochondria within hundreds of single cells from early infection to syncytia formation and death. SARS-CoV-2 infection enlarges nucleoli, perturbs LD, changes mitochondrial shape and dry mass, and separates LD from mitochondria. We then used Bayesian statistics on organelle dry mass states to define organelle cross-regulation (OCR) networks and report modifications of OCR that are triggered by infection and syncytia formation. Our work highlights the subcellular remodeling induced by SARS-CoV-2 infection and provides a new AI-enhanced, label-free methodology to study in real-time the dynamics of cell populations and their content.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2023-11-17
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2023.11.16.567378
    Datenquelle COVID19

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  3. Artikel ; Online: The Spike-Stabilizing D614G Mutation Interacts with S1/S2 Cleavage Site Mutations To Promote the Infectious Potential of SARS-CoV-2 Variants.

    Gellenoncourt, Stacy / Saunders, Nell / Robinot, Rémy / Auguste, Lucas / Rajah, Maaran Michael / Kervevan, Jérôme / Jeger-Madiot, Raphaël / Staropoli, Isabelle / Planchais, Cyril / Mouquet, Hugo / Buchrieser, Julian / Schwartz, Olivier / Chakrabarti, Lisa A

    Journal of virology

    2022  Band 96, Heft 19, Seite(n) e0130122

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) remained genetically stable during the first 3 months of the pandemic, before acquiring a D614G spike mutation that rapidly spread worldwide and then generating successive waves of viral ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) remained genetically stable during the first 3 months of the pandemic, before acquiring a D614G spike mutation that rapidly spread worldwide and then generating successive waves of viral variants with increasingly high transmissibility. We set out to evaluate possible epistatic interactions between the early-occurring D614G mutation and the more recently emerged cleavage site mutations present in spike of the Alpha, Delta, and Omicron variants of concern. The P681H/R mutations at the S1/S2 cleavage site increased spike processing and fusogenicity but limited its incorporation into pseudoviruses. In addition, the higher cleavage rate led to higher shedding of the spike S1 subunit, resulting in a lower infectivity of the P681H/R-carrying pseudoviruses compared to those expressing the Wuhan wild-type spike. The D614G mutation increased spike expression at the cell surface and limited S1 shedding from pseudovirions. As a consequence, the D614G mutation preferentially increased the infectivity of P681H/R-carrying pseudoviruses. This enhancement was more marked in cells where the endosomal route predominated, suggesting that more stable spikes could better withstand the endosomal environment. Taken together, these findings suggest that the D614G mutation stabilized S1/S2 association and enabled the selection of mutations that increased S1/S2 cleavage, leading to the emergence of SARS-CoV-2 variants expressing highly fusogenic spikes.
    Mesh-Begriff(e) COVID-19/virology ; Humans ; Mutation ; SARS-CoV-2/genetics ; SARS-CoV-2/pathogenicity ; Spike Glycoprotein, Coronavirus/genetics
    Chemische Substanzen Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Sprache Englisch
    Erscheinungsdatum 2022-09-19
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01301-22
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  4. Artikel ; Online: The spike-stabilizing D614G mutation interacts with S1/S2 cleavage site mutations to promote the infectious potential of SARS-CoV-2 variants

    Gellenoncourt, Stacy / Saunders, Nell / Robinot, Remy / Auguste, Lucas / Rajah, Maaran Michael / Kervevan, Jerome / Jeger-Madiot, Raphael / Staropoli, Isabelle / Planchais, Cyril / Mouquet, Hugo / Buchrieser, Julian / Schwartz, Olivier / Chakrabarti, Lisa A.

    bioRxiv

    Abstract: SARS-CoV-2 remained genetically stable during the first three months of the pandemic, before acquiring a D614G spike mutation that rapidly spread worldwide, and then generating successive waves of viral variants with increasingly high transmissibility. ... ...

    Abstract SARS-CoV-2 remained genetically stable during the first three months of the pandemic, before acquiring a D614G spike mutation that rapidly spread worldwide, and then generating successive waves of viral variants with increasingly high transmissibility. We set out to evaluate possible epistatic interactions between the early occurring D614G mutation and the more recently emerged cleavage site mutations present in spike of the Alpha, Delta, and Omicron variants of concern. The P681H/R mutations at the S1/S2 cleavage site increased spike processing and fusogenicity but limited its incorporation into pseudoviruses. In addition, the higher cleavage rate led to higher shedding of the spike S1 subunit, resulting in a lower infectivity of the P681H/R-carrying pseudoviruses compared to those expressing the Wuhan wild-type spike. The D614G mutation increased spike expression at the cell surface and limited S1 shedding from pseudovirions. As a consequence, the D614G mutation preferentially increased the infectivity of P681H/R-carrying pseudoviruses. This enhancement was more marked in cells where the endosomal route predominated, suggesting that more stable spikes could better withstand the endosomal environment. Taken together, these findings suggest that the D614G mutation stabilized S1/S2 association and enabled the selection of mutations that increased S1/S2 cleavage, leading to the emergence of SARS-CoV-2 variants expressing highly fusogenic spikes.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2022-05-20
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2022.05.20.492832
    Datenquelle COVID19

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  5. Artikel ; Online: A Nanoprimer To Improve the Systemic Delivery of siRNA and mRNA.

    Saunders, Nell R M / Paolini, Marion S / Fenton, Owen S / Poul, Laurence / Devalliere, Julie / Mpambani, Francis / Darmon, Audrey / Bergère, Maxime / Jibault, Océane / Germain, Matthieu / Langer, Robert

    Nano letters

    2020  Band 20, Heft 6, Seite(n) 4264–4269

    Abstract: Despite tremendous interest in gene therapies, the systemic delivery of nucleic acids still faces substantial challenges. To successfully administer nucleic acids, one approach is to encapsulate them in lipid nanoparticles (LNPs). However, LNPs ... ...

    Abstract Despite tremendous interest in gene therapies, the systemic delivery of nucleic acids still faces substantial challenges. To successfully administer nucleic acids, one approach is to encapsulate them in lipid nanoparticles (LNPs). However, LNPs administered intravenously substantially accumulate in the liver where they are taken up by the reticuloendothelial system (RES). Here, we administer prior to the LNPs a liposome designed to transiently occupy liver cells, the Nanoprimer. This study demonstrates that the pretreatment of mice with the Nanoprimer decreases the LNPs' uptake by the RES. By accumulating rapidly in the liver cells, the Nanoprimer improves the bioavailability of the LNPs encapsulating human erythropoietin (hEPO) mRNA or factor VII (FVII) siRNA, leading respectively to more hEPO production (by 32%) or FVII silencing (by 49%). The use of the Nanoprimer offers a new strategy to improve the systemic delivery of RNA-based therapeutics.
    Mesh-Begriff(e) Animals ; Drug Delivery Systems ; Hepatocytes ; Lipids ; Mice ; Nanoparticles ; RNA, Messenger/genetics ; RNA, Small Interfering/genetics
    Chemische Substanzen Lipids ; RNA, Messenger ; RNA, Small Interfering
    Sprache Englisch
    Erscheinungsdatum 2020-05-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1530-6992
    ISSN (online) 1530-6992
    DOI 10.1021/acs.nanolett.0c00752
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: SARS-CoV-2 Alpha, Beta, and Delta variants display enhanced Spike-mediated syncytia formation.

    Rajah, Maaran Michael / Hubert, Mathieu / Bishop, Elodie / Saunders, Nell / Robinot, Remy / Grzelak, Ludivine / Planas, Delphine / Dufloo, Jérémy / Gellenoncourt, Stacy / Bongers, Alice / Zivaljic, Marija / Planchais, Cyril / Guivel-Benhassine, Florence / Porrot, Françoise / Mouquet, Hugo / Chakrabarti, Lisa A / Buchrieser, Julian / Schwartz, Olivier

    The EMBO journal

    2021  Band 40, Heft 24, Seite(n) e108944

    Abstract: Severe COVID-19 is characterized by lung abnormalities, including the presence of syncytial pneumocytes. Syncytia form when SARS-CoV-2 spike protein expressed on the surface of infected cells interacts with the ACE2 receptor on neighboring cells. The ... ...

    Abstract Severe COVID-19 is characterized by lung abnormalities, including the presence of syncytial pneumocytes. Syncytia form when SARS-CoV-2 spike protein expressed on the surface of infected cells interacts with the ACE2 receptor on neighboring cells. The syncytia forming potential of spike variant proteins remain poorly characterized. Here, we first assessed Alpha (B.1.1.7) and Beta (B.1.351) spread and fusion in cell cultures, compared with the ancestral D614G strain. Alpha and Beta replicated similarly to D614G strain in Vero, Caco-2, Calu-3, and primary airway cells. However, Alpha and Beta formed larger and more numerous syncytia. Variant spike proteins displayed higher ACE2 affinity compared with D614G. Alpha, Beta, and D614G fusion was similarly inhibited by interferon-induced transmembrane proteins (IFITMs). Individual mutations present in Alpha and Beta spikes modified fusogenicity, binding to ACE2 or recognition by monoclonal antibodies. We further show that Delta spike also triggers faster fusion relative to D614G. Thus, SARS-CoV-2 emerging variants display enhanced syncytia formation.
    Mesh-Begriff(e) Angiotensin-Converting Enzyme 2/metabolism ; Animals ; Antibodies, Monoclonal/pharmacology ; Caco-2 Cells ; Cell Line ; Chlorocebus aethiops ; Giant Cells/drug effects ; Giant Cells/metabolism ; Giant Cells/virology ; HEK293 Cells ; Humans ; Mutation ; SARS-CoV-2/drug effects ; SARS-CoV-2/genetics ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/genetics ; Vero Cells ; Virus Replication/drug effects
    Chemische Substanzen Antibodies, Monoclonal ; 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)
    Sprache Englisch
    Erscheinungsdatum 2021-10-25
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2021108944
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  7. Artikel ; Online: Fusogenicity and neutralization sensitivity of the SARS-CoV-2 Delta sublineage AY.4.2.

    Saunders, Nell / Planas, Delphine / Bolland, William H / Rodriguez, Christophe / Fourati, Slim / Buchrieser, Julian / Planchais, Cyril / Prot, Matthieu / Staropoli, Isabelle / Guivel-Benhassine, Florence / Porrot, Françoise / Veyer, David / Péré, Hélène / Robillard, Nicolas / Saliba, Madelina / Baidaliuk, Artem / Seve, Aymeric / Hocqueloux, Laurent / Prazuck, Thierry /
    Rey, Felix A / Mouquet, Hugo / Simon-Lorière, Etienne / Bruel, Timothée / Pawlotsky, Jean-Michel / Schwartz, Olivier

    EBioMedicine

    2022  Band 77, Seite(n) 103934

    Abstract: Background: SARS-CoV-2 lineages are continuously evolving. As of December 2021, the AY.4.2 Delta sub-lineage represented 20 % of sequenced strains in the UK and had been detected in dozens of countries. It has since then been supplanted by Omicron. The ... ...

    Abstract Background: SARS-CoV-2 lineages are continuously evolving. As of December 2021, the AY.4.2 Delta sub-lineage represented 20 % of sequenced strains in the UK and had been detected in dozens of countries. It has since then been supplanted by Omicron. The AY.4.2 spike displays three additional mutations (T95I, Y145H and A222V) in the N-terminal domain when compared to the original Delta variant (B.1.617.2) and remains poorly characterized.
    Methods: We compared the Delta and the AY.4.2 spikes, by assessing their binding to antibodies and ACE2 and their fusogenicity. We studied the sensitivity of an authentic AY.4.2 viral isolate to neutralizing antibodies.
    Findings: The AY.4.2 spike exhibited similar binding to all the antibodies and sera tested, and similar fusogenicity and binding to ACE2 than the ancestral Delta spike. The AY.4.2 virus was slightly less sensitive than Delta to neutralization by a panel of monoclonal antibodies; noticeably, the anti-RBD Imdevimab showed incomplete neutralization. Sensitivity of AY.4.2 to sera from vaccinated individuals was reduced by 1.3 to 3-fold, when compared to Delta.
    Interpretation: Our results suggest that mutations in the NTD remotely impair the efficacy of anti-RBD antibodies. The spread of AY.4.2 was not due to major changes in spike fusogenicity or ACE2 binding, but more likely to a partially reduced neutralization sensitivity.
    Funding: The work was funded by Institut Pasteur, Fondation pour la Recherche Médicale, Urgence COVID-19 Fundraising Campaign of Institut Pasteur, ANRS, the Vaccine Research Institute, Labex IBEID, ANR/FRM Flash Covid PROTEO-SARS-CoV-2 and IDISCOVR.
    Mesh-Begriff(e) Antibodies, Monoclonal, Humanized ; Antibodies, Viral ; COVID-19 ; Humans ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/genetics ; Viral Envelope Proteins
    Chemische Substanzen Antibodies, Monoclonal, Humanized ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; spike protein, SARS-CoV-2 ; imdevimab (2Z3DQD2JHM)
    Sprache Englisch
    Erscheinungsdatum 2022-03-13
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 2851331-9
    ISSN 2352-3964
    ISSN (online) 2352-3964
    DOI 10.1016/j.ebiom.2022.103934
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  8. Artikel ; Online: TMPRSS2 is a functional receptor for human coronavirus HKU1.

    Saunders, Nell / Fernandez, Ignacio / Planchais, Cyril / Michel, Vincent / Rajah, Maaran Michael / Baquero Salazar, Eduard / Postal, Jeanne / Porrot, Francoise / Guivel-Benhassine, Florence / Blanc, Catherine / Chauveau-Le Friec, Gaëlle / Martin, Augustin / Grzelak, Ludivine / Oktavia, Rischa Maya / Meola, Annalisa / Ahouzi, Olivia / Hoover-Watson, Hunter / Prot, Matthieu / Delaune, Deborah /
    Cornelissen, Marion / Deijs, Martin / Meriaux, Véronique / Mouquet, Hugo / Simon-Lorière, Etienne / van der Hoek, Lia / Lafaye, Pierre / Rey, Felix / Buchrieser, Julian / Schwartz, Olivier

    Nature

    2023  Band 624, Heft 7990, Seite(n) 207–214

    Abstract: Four endemic seasonal human coronaviruses causing common colds circulate worldwide: HKU1, 229E, NL63 and OC43 (ref. ...

    Abstract Four endemic seasonal human coronaviruses causing common colds circulate worldwide: HKU1, 229E, NL63 and OC43 (ref.
    Mesh-Begriff(e) Humans ; Betacoronavirus/metabolism ; Bronchi/cytology ; Bronchi/virology ; Common Cold/drug therapy ; Common Cold/virology ; Membrane Fusion ; Receptors, Virus/metabolism ; SARS-CoV-2 ; Serine Endopeptidases/metabolism ; Single-Domain Antibodies/pharmacology ; Single-Domain Antibodies/therapeutic use ; Species Specificity ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Internalization
    Chemische Substanzen Receptors, Virus ; Serine Endopeptidases (EC 3.4.21.-) ; Single-Domain Antibodies ; Spike Glycoprotein, Coronavirus ; TMPRSS2 protein, human (EC 3.4.21.-)
    Sprache Englisch
    Erscheinungsdatum 2023-10-25
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06761-7
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  9. Artikel ; Online: B.1.1.7 and B.1.351 SARS-CoV-2 variants display enhanced Spike-mediated fusion

    Rajah, Maaran Michael / Hubert, Mathieu / Bishop, Elodie / Saunders, Nell / Robinot, Rémy / Grzelak, Ludivine / Planas, Delphine / Zivaljic, Marija / Planchais, Cyril / Guivel-Benhassine, Florence / Porrot, Françoise / Mouquet, Hugo / Chakrabarti, Lisa / Buchrieser, Julian / Schwartz, Olivier

    bioRxiv

    Abstract: SARS-CoV-2 B.1.1.7 (variant Alpha) and B.1.351 (variant Beta) have supplanted pre-existing strains in many countries. Severe COVID-19 is characterized by lung abnormalities, including the presence of syncytial pneumocytes. Syncytia form when infected ... ...

    Abstract SARS-CoV-2 B.1.1.7 (variant Alpha) and B.1.351 (variant Beta) have supplanted pre-existing strains in many countries. Severe COVID-19 is characterized by lung abnormalities, including the presence of syncytial pneumocytes. Syncytia form when infected cells fuse with adjacent cells. The fitness, cytopathic effects and type-I interferon (IFN) sensitivity of the variants remain poorly characterized. Here, we assessed B.1.1.7 and B.1.351 spread and fusion in cell cultures. B.1.1.7 and B.1.351 replicated similarly to D614G reference strain in Vero, Caco-2, Calu-3 and primary airway cells and were similarly sensitive to IFN. The variants formed larger and more numerous syncytia. Variant Spikes, in the absence of any other viral proteins, resulted in faster fusion relative to D614G. B.1.1.7 and B.1.351 fusion was similarly inhibited by interferon induced transmembrane proteins (IFITMs). Individual mutations present in the variant Spikes modified fusogenicity, binding to ACE2 and recognition by monoclonal antibodies. Also, B.1.1.7 and B.1.351 variants remain sensitive to innate immunity components. The mutations present in the two variants globally enhance viral fusogenicity and allow for antibody evasion.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2021-06-11
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2021.06.11.448011
    Datenquelle COVID19

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  10. Artikel ; Online: Fusogenicity and neutralization sensitivity of the SARS-CoV-2 Delta sublineage AY.4.2

    Saunders, Nell / Planas, Delphine / Bolland, William Henry / Rodriguez, Christophe / Fourati, Slim / Buchrieser, Julian / Planchais, Cyril / Prot, Matthieu / Staropoli, Isabelle / Guivel-Benhassine, Florence / Porrot, Francoise / Veyer, David / Pere, Helene / Robillard, Nicolas / Saliba, Madelina / Baidaliuk, Artem / Seve, Aymeric / Hocqueloux, Laurent / Prazuck, Thierry /
    Mouquet, Hugo / Simon-Loriere, Etienne / Bruel, Timothee / Pawlotsky, Jean-Michel / Schwartz, Olivier

    bioRxiv

    Abstract: SARS-CoV-2 lineages are continuously evolving. As of December 2021, the AY.4.2 Delta sub-lineage represented 20 % of sequenced strains in UK and has been detected in dozens of countries. It has since then been supplanted by the Omicron variant. AY.4.2 ... ...

    Abstract SARS-CoV-2 lineages are continuously evolving. As of December 2021, the AY.4.2 Delta sub-lineage represented 20 % of sequenced strains in UK and has been detected in dozens of countries. It has since then been supplanted by the Omicron variant. AY.4.2 displays three additional mutations (T95I, Y145H and A222V) in the N-terminal domain (NTD) of the spike when compared to the original Delta variant (B.1.617.2) and remains poorly characterized. Here, we analyzed the fusogenicity of the AY.4.2 spike and the sensitivity of an authentic AY.4.2 isolate to neutralizing antibodies. The AY.4.2 spike exhibited similar fusogenicity and binding to ACE2 than Delta. The sensitivity of infectious AY.4.2 to a panel of monoclonal neutralizing antibodies was similar to Delta, except for the anti-RBD Imdevimab, which showed incomplete neutralization. Sensitivity of AY.4.2 to sera from individuals having received two or three doses of Pfizer or two doses of AstraZeneca vaccines was reduced by 1.7 to 2.1 fold, when compared to Delta. Our results suggest that mutations in the NTD remotely impair the efficacy of anti-RBD antibodies. The temporary spread of AY.4.2 was not associated with major changes in spike function but rather to a partially reduced neutralization sensitivity.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2022-01-10
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2022.01.07.475248
    Datenquelle COVID19

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