Efficient Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by the Transmembrane Protease TMPRSS2

By S. Matsuyama, N. Nagata, K. Shirato, Miyuki Kawase, M. Takeda, F. Taguchi. Journal of Virology, 2010

738 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/8fc613ca5ed764201a1cfebcfe0255c765e1fa82

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In Infectious Diseases

Citations in the corpus

Coronavirus Pathogenesis (2011, background): “, 2005) and the serine protease TMPRSS2 (Matsuyama et al., 2010; Shulla et al., 2011) have been reported to affect SARS-CoV entry through cleavage of the spike protein and activation of its membrane fusion activity.”
The protein expression profile of ACE2 in human tissues (2020, neutral): “SARS-CoV has previously been shown to enter the cell via the ACE2 receptor, primed by the cellular serine protease TMPRSS2 (Li et al , 2005; Matsuyama et al , 2010).”
Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells (2020, background): “Data for SARS-CoV show that TMPRSS2 enhances its entry efficiency (5, 11) .”
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] .”
TMPRSS2 and ADAM17 Cleave ACE2 Differentially and Only Proteolysis by TMPRSS2 Augments Entry Driven by the Severe Acute Respiratory Syndrome Coronavirus Spike Protein (2013, background): “Both TMPRSS2 and HAT are expressed in ACE2-positive cells in the human lung (27, 29), and results obtained with surrogate cell culture systems suggest that TMPRSS2 might play a significant role in SARS-CoV spread in the human respiratory tract (30).”
A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells (2020, positive): “Our previous work revealed that the activity of the cellular serine protease TMPRSS2, which activates several coronaviruses (Bertram et al., 2013; Gierer et al., 2013; Glowacka et al., 2011; Matsuyama et al., 2010; Shirato et al., 2013, 2016; Shulla et al., 2011), is also required for robust SARS-Co”
SARS-CoV-2 Reverse Genetics Reveals a Variable Infection Gradient in the Respiratory Tract (2020, background): “…cell surface and intracellular proteases, play an essential role in CoV infection by processing the S protein to trigger membrane fusion (Izaguirre, 2019; Matsuyama et al., 2010; Matsuyama et al., 2005; Menachery et al., (A) Full-length cDNA clone constructs and genomes of recombinant viruses.”
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein (2020, background): “The presence of a furin cleavage site sets SARS-CoV-2 S apart from SARS-CoV S (and SARSr-CoV S) that possesses a monobasic S1/S2 cleavage site processed upon entry of target cells (Belouzard et al., 2009; Bosch et al., 2008; Glowacka et al., 2011; Matsuyama et al., 2010; Millet and Whittaker, 2015; ”