SARS-CoV-2 spike engagement of ACE2 primes S2′ site cleavage and fusion initiation
Published 2021 View Full Article
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Title
SARS-CoV-2 spike engagement of ACE2 primes S2′ site cleavage and fusion initiation
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 119, Issue 1, Pages e2111199119
Publisher
Proceedings of the National Academy of Sciences
Online
2021-12-21
DOI
10.1073/pnas.2111199119
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Note: Only part of the references are listed.- Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis
- (2021) Bryan A. Johnson et al. NATURE
- Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion
- (2021) Guido Papa et al. PLoS Pathogens
- SARS-CoV-2 variants with mutations at the S1/S2 cleavage site are generated in vitro during propagation in TMPRSS2-deficient cells
- (2021) Michihito Sasaki et al. PLoS Pathogens
- SARS-CoV-2 entry into human airway organoids is serine protease-mediated and facilitated by the multibasic cleavage site
- (2021) Anna Z Mykytyn et al. eLife
- Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with proteins related to the renin-angiotensin system
- (2021) Man Lung Yeung et al. CELL
- SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on Ca2+
- (2021) Alex L. Lai et al. JOURNAL OF MOLECULAR BIOLOGY
- Clofazimine broadly inhibits coronaviruses including SARS-CoV-2
- (2021) Shuofeng Yuan et al. NATURE
- Drugs that inhibit TMEM16 proteins block SARS-CoV-2 spike-induced syncytia
- (2021) Luca Braga et al. NATURE
- Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies
- (2021) Delphine Planas et al. NATURE MEDICINE
- Human airway cells prevent SARS-CoV-2 multibasic cleavage site cell culture adaptation
- (2021) Mart M Lamers et al. eLife
- The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets
- (2021) Thomas P. Peacock et al. Nature Microbiology
- A pneumonia outbreak associated with a new coronavirus of probable bat origin
- (2020) Peng Zhou et al. NATURE
- Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
- (2020) Daniel Wrapp et al. SCIENCE
- SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
- (2020) Markus Hoffmann et al. CELL
- A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells
- (2020) Markus Hoffmann et al. MOLECULAR CELL
- Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
- (2020) Jun Lan et al. NATURE
- Structural basis of receptor recognition by SARS-CoV-2
- (2020) Jian Shang et al. NATURE
- Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus
- (2020) Bette Korber et al. CELL
- SARS-coronavirus-2 replication in Vero E6 cells: replication kinetics, rapid adaptation and cytopathology
- (2020) Natacha S. Ogando et al. JOURNAL OF GENERAL VIROLOGY
- The protein expression profile of ACE2 in human tissues
- (2020) Feria Hikmet et al. Molecular Systems Biology
- Discovery of SARS-CoV-2 antiviral drugs through large-scale compound repurposing
- (2020) Laura Riva et al. NATURE
- Distinct conformational states of SARS-CoV-2 spike protein
- (2020) Yongfei Cai et al. SCIENCE
- Morphogenesis and cytopathic effect of SARS-CoV-2 infection in human airway epithelial cells
- (2020) Na Zhu et al. Nature Communications
- Syncytia formation by SARS‐CoV‐2 infected cells
- (2020) Julian Buchrieser et al. EMBO JOURNAL
- Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
- (2020) Donald J. Benton et al. NATURE
- Structures and distributions of SARS-CoV-2 spike proteins on intact virions
- (2020) Zunlong Ke et al. NATURE
- Spike mutation D614G alters SARS-CoV-2 fitness
- (2020) Jessica A. Plante et al. NATURE
- Neuropilin-1 is a host factor for SARS-CoV-2 infection
- (2020) James L. Daly et al. SCIENCE
- Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity
- (2020) Ludovico Cantuti-Castelvetri et al. SCIENCE
- Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects
- (2020) Ya-Wen Cheng et al. Cell Reports
- Opposing activities of IFITM proteins in SARS‐CoV‐2 infection
- (2020) Guoli Shi et al. EMBO JOURNAL
- SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
- (2020) Lizhou Zhang et al. Nature Communications
- Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
- (2019) Alexandra C. Walls et al. CELL
- Functional analysis of potential cleavage sites in the MERS-coronavirus spike protein
- (2018) Hannah Kleine-Weber et al. Scientific Reports
- The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner
- (2017) Alex L. Lai et al. JOURNAL OF MOLECULAR BIOLOGY
- Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
- (2017) Alexandra C. Walls et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structure, Function, and Evolution of Coronavirus Spike Proteins
- (2016) Fang Li Annual Review of Virology
- A Serpin Shapes the Extracellular Environment to Prevent Influenza A Virus Maturation
- (2015) Meike Dittmann et al. CELL
- Identification and Characterization of a Proteolytically Primed Form of the Murine Coronavirus Spike Proteins after Fusion with the Target Cell
- (2014) O. Wicht et al. JOURNAL OF VIROLOGY
- Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein
- (2014) Jean Kaoru Millet et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- TMPRSS2 and ADAM17 Cleave ACE2 Differentially and Only Proteolysis by TMPRSS2 Augments Entry Driven by the Severe Acute Respiratory Syndrome Coronavirus Spike Protein
- (2013) A. Heurich et al. JOURNAL OF VIROLOGY
- Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease
- (2011) S. Bertram et al. JOURNAL OF VIROLOGY
- Evidence that TMPRSS2 Activates the Severe Acute Respiratory Syndrome Coronavirus Spike Protein for Membrane Fusion and Reduces Viral Control by the Humoral Immune Response
- (2011) I. Glowacka et al. JOURNAL OF VIROLOGY
- Elastase-mediated Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein at Discrete Sites within the S2 Domain
- (2010) Sandrine Belouzard et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Transmembrane Serine Protease Is Linked to the Severe Acute Respiratory Syndrome Coronavirus Receptor and Activates Virus Entry
- (2010) A. Shulla et al. JOURNAL OF VIROLOGY
- Efficient Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by the Transmembrane Protease TMPRSS2
- (2010) S. Matsuyama et al. JOURNAL OF VIROLOGY
- Two-Step Conformational Changes in a Coronavirus Envelope Glycoprotein Mediated by Receptor Binding and Proteolysis
- (2009) S. Matsuyama et al. JOURNAL OF VIROLOGY
- Characterization of a Highly Conserved Domain within the Severe Acute Respiratory Syndrome Coronavirus Spike Protein S2 Domain with Characteristics of a Viral Fusion Peptide
- (2009) I. G. Madu et al. JOURNAL OF VIROLOGY
- Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
- (2009) S. Belouzard et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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