Details

Autor(en) / Beteiligte

• 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

Titel

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Ist Teil von

• Nature communications, 2021-11, Vol.12 (1), p.6855-6855, Article 6855

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2021

Link zum Volltext

Quelle

Electronic Journals Library - Freely accessible e-journals

Beschreibungen/Notizen

• 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.