SARS-CoV-2 variants with mutations at the S1/S2 cleavage site are generated in vitro during propagation in TMPRSS2-deficient cells

• Published in: PLoS pathogens Vol. 17; no. 1; p. e1009233
• Main Authors: Sasaki, Michihito, Uemura, Kentaro, Sato, Akihiko, Toba, Shinsuke, Sanaki, Takao, Maenaka, Katsumi, Hall, William W., Orba, Yasuko, Sawa, Hirofumi
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 21.01.2021; Public Library of Science (PLoS)
• Subjects: ACE2; Amino Acid Sequence; Amino acids; Analysis; Angiotensin; Angiotensin-converting enzyme 2; Animals; Binding sites; Biology and life sciences; Caco-2 Cells; Cell Line; Chlorocebus aethiops; Cleavage; Cloning; Coronaviruses; COVID-19; Dilution; Gene mutations; Genetic aspects; Genomes; HEK293 Cells; Humans; Infections; Medicine and health sciences; Mutation; Nucleotides; Pandemics; Peptidyl-dipeptidase A; Progeny; Propagation; Proteins; Receptors; Research and Analysis Methods; S gene; SARS-CoV-2 - classification; SARS-CoV-2 - genetics; SARS-CoV-2 - growth & development; SARS-CoV-2 - physiology; Sequence Alignment; Serial Passage; Serine Endopeptidases - deficiency; Severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; Spike Glycoprotein, Coronavirus - genetics; Vero Cells; Viral diseases; Viral Tropism; Virions; Viruses; Japan

The spike (S) protein of Severe Acute Respiratory Syndrome-Coronavirus-2 (SARS-CoV-2) binds to a host cell receptor which facilitates viral entry. A polybasic motif detected at the cleavage site of the S protein has been shown to broaden the cell tropism and transmissibility of the virus. Here we ex...