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Zech, Fabian; Schniertshauer, Daniel; Jung, Christoph; Herrmann, Alexandra; Cordsmeier, Arne; Xie, Qinya; Nchioua, Rayhane; Prelli Bozzo, Caterina; Volcic, Meta; Koepke, Lennart; Müller, Janis A; Krüger, Jana; Heller, Sandra; Stenger, Steffen; Hoffmann, Markus; Pöhlmann, Stefan; Kleger, Alexander; Jacob, Timo; Conzelmann, Karl-Klaus; Ensser, Armin; Sparrer, Konstantin M J; Kirchhoff, Frank
Nature communications, 11/2021, Letnik: 12, Številka: 1Journal Article
The bat sarbecovirus RaTG13 is a close relative of SARS-CoV-2, the cause of the COVID-19 pandemic. However, this bat virus was most likely unable to directly infect humans since its Spike (S) protein does not interact efficiently with the human ACE2 receptor. Here, we show that a single T403R mutation increases binding of RaTG13 S to human ACE2 and allows VSV pseudoparticle infection of human lung cells and intestinal organoids. Conversely, mutation of R403T in the SARS-CoV-2 S reduces pseudoparticle infection and viral replication. The T403R RaTG13 S is neutralized by sera from individuals vaccinated against COVID-19 indicating that vaccination might protect against future zoonoses. Our data suggest that a positively charged amino acid at position 403 in the S protein is critical for efficient utilization of human ACE2 by S proteins of bat coronaviruses. This finding could help to better predict the zoonotic potential of animal coronaviruses.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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