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

Saunders, Nell / Schwartz, Olivier

2024 Volume 40, Issue 4, Page(s) 335–337

Title translation	TMPRSS2 is the receptor of seasonal coronavirus HKU1.
MeSH term(s)	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
Chemical Substances	TMPRSS2 protein, human (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Receptors, Virus
Language	French
Publishing date	2024-04-23
Publishing country	France
Document type	News ; Journal Article
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2024034
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Article ; 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.
Keywords	covid19
Language	English
Publishing date	2023-11-17
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.11.16.567378
Database	COVID19

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Article ; 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 Volume 96, Issue 19, Page(s) 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 term(s)	COVID-19/virology ; Humans ; Mutation ; SARS-CoV-2/genetics ; SARS-CoV-2/pathogenicity ; Spike Glycoprotein, Coronavirus/genetics
Chemical Substances	Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-09-19
Publishing country	United States
Document type	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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Article ; 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.
Keywords	covid19
Language	English
Publishing date	2022-05-20
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.05.20.492832
Database	COVID19

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Article ; 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 Volume 20, Issue 6, Page(s) 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 term(s)	Animals ; Drug Delivery Systems ; Hepatocytes ; Lipids ; Mice ; Nanoparticles ; RNA, Messenger/genetics ; RNA, Small Interfering/genetics
Chemical Substances	Lipids ; RNA, Messenger ; RNA, Small Interfering
Language	English
Publishing date	2020-05-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1530-6992
ISSN (online)	1530-6992
DOI	10.1021/acs.nanolett.0c00752
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Article ; 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 Volume 40, Issue 24, Page(s) 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 term(s)	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
Chemical Substances	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)
Language	English
Publishing date	2021-10-25
Publishing country	England
Document type	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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Article ; 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 Volume 77, Page(s) 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 term(s)	Antibodies, Monoclonal, Humanized ; Antibodies, Viral ; COVID-19 ; Humans ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/genetics ; Viral Envelope Proteins
Chemical Substances	Antibodies, Monoclonal, Humanized ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; spike protein, SARS-CoV-2 ; imdevimab (2Z3DQD2JHM)
Language	English
Publishing date	2022-03-13
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2022.103934
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Article ; 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 Volume 624, Issue 7990, Page(s) 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 term(s)	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
Chemical Substances	Receptors, Virus ; Serine Endopeptidases (EC 3.4.21.-) ; Single-Domain Antibodies ; Spike Glycoprotein, Coronavirus ; TMPRSS2 protein, human (EC 3.4.21.-)
Language	English
Publishing date	2023-10-25
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/s41586-023-06761-7
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Article ; 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.
Keywords	covid19
Language	English
Publishing date	2021-06-11
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.06.11.448011
Database	COVID19

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Article ; 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.
Keywords	covid19
Language	English
Publishing date	2022-01-10
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.01.07.475248
Database	COVID19

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