Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites

By S. Belouzard, Victor C. Chu, Gary R. Whittaker. Proceedings of the National Academy of Sciences of the United States of America, 2009

994 citations recorded by the source corpus.

Subfields: Genetics, Infectious Diseases

View Paper: https://www.semanticscholar.org/paper/a96000bba6cc98ded3d2c5a96158d9b9502ed94f

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Citations in the corpus

The deadly coronaviruses: The 2003 SARS pandemic and the 2020 novel coronavirus epidemic in China (2020, neutral): “Upon binding the receptor, the spike protein is cleaved by nearby host proteases and releases the signal peptide to facilitate virus entry into host cells [112] [113] [114] [115] .”
Murine Leukemia Virus (MLV)-based Coronavirus Spike-pseudotyped Particle Production and Infection (2016, methodology): “It has been extensively used in our research on viral entry of various enveloped viruses, including VSV (Sun et al., 2008), influenza virus (Tse et al., 2014) and coronaviruses (Belouzard et al., 2009; Millet and Whittaker 2014; Millet et al., 2016).”
Coronavirus Pathogenesis (2011, background): “Whittaker and coworkers proposed that there are two critical cleavage events, one at the S1/S1 boundary and the other within S2 at R797 which act in concert to mediate membrane fusion and virus infectivity (Belouzard et al., 2009 (Belouzard et al., , 2010 .”
Distinct Patterns of IFITM-Mediated Restriction of Filoviruses, SARS Coronavirus, and Influenza A Virus (2011, background): “Proteolytic cleavage of these entry proteins by lysosomal cathepsin L (SARS-CoV) or cathepsins B and L (Ebola virus; EBOV) promotes the final steps of viral fusion [14,15].”
Coronaviruses: An Overview of Their Replication and Pathogenesis (2015, background): “S protein cleavage occurs at two sites within the S2 portion of the protein, with the fi rst cleavage important for separating the RBD and fusion domains of the S protein [ 31 ] and Table 1”
Efficient Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by the Transmembrane Protease TMPRSS2 (2010, background): “The protease cleavage site in S protein, located nearer the C-terminal region than predicted for a cleavage site, is thought to be exposed only after receptor binding (2, 35).”
Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections (2017, background): “6 For a subset of coronaviruses, such as MHV, SARS-CoV and MERS-CoV, the S 116 glycoprotein is cleaved at the S1/S2 junction during biogenesis and viral egress(10-13).”
Human Coronavirus: Host-Pathogen Interaction. (2019, background): “For instance, activation of SARS-CoV S protein requires sequential cleavage by the endosomal cysteine protease cathepsin L (7, 105) and another trypsin-like serine protease (4).”
Molecular immune pathogenesis and diagnosis of COVID-19 (2020, positive): “Belouzard et al.[20] found that a critical proteolytic cleavage event oc curred at SARS-CoV S protein at position (S2') mediated the membrane fusion and viral infectivity.”
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion (2020, positive): “…S cleavage by host proteases at the boundary between the S1 and S2 subunits (S1/S2), in a subset of coronaviruses, and at a conserved site upstream of the fusion peptide (S2’) in all known coronaviruses (Belouzard et al., 2009; Burkard et al., 2014; Millet and Whittaker, 2014; Park et al., 2016).”
Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein (2014, background): “Another finding, by Belouzard and colleagues (11), is that pseudovirions harboring S with point mutations, and in particular the SARS-CoV R797N S2′ site mutation, still retained infectivity close to that observed with wt S.”