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Spike residue 403 affects binding of coronavirus spikes to human ACE2

Medicine and Health

Spike residue 403 affects binding of coronavirus spikes to human ACE2

F. Zech, D. Schnierthauer, et al.

This research by Fabian Zech and colleagues reveals how a single T403R mutation in the bat sarbecovirus RaTG13's Spike protein enhances its ability to infect human cells. The findings suggest that current COVID-19 vaccines provide a layer of protection against potential zoonotic threats, highlighting the importance of amino acid interactions in cross-species virus transmission.

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Playback language: English
Abstract
The bat sarbecovirus RaTG13, a close relative of SARS-CoV-2, likely couldn't directly infect humans due to its Spike (S) protein's inefficient interaction with human ACE2. A single T403R mutation in RaTG13 S increases its binding to human ACE2, enabling infection of human lung cells and intestinal organoids. Conversely, R403T mutation in SARS-CoV-2 S reduces infection. COVID-19 vaccine sera neutralize T403R RaTG13 S, suggesting vaccine protection against future zoonotic events. A positively charged amino acid at position 403 in the S protein is crucial for bat coronavirus S proteins to use human ACE2.
Publisher
Nature Communications
Published On
Nov 16, 2021
Authors
Fabian Zech, Daniel Schnierthauer, Christoph Jung, Alexandra Herrmann, Arne Cordsmeier, Qinya Xie, Rayhane Nchioua, Caterina Prelli Bozzo, Meta Volcic, Lennart Koepke, Janis A Müller, Jana Krüger, Sandra Heller, Steffen Stenger, Markus Hoffmann, Stefan Pöhlmann, Alexander Kleger, Timo Jacob, Karl-Klaus Conzelmann, Armin Enserink, Konstantin M J Sparrer, Frank Kirchhoff
Tags
bat sarbecovirus
RaTG13
Spike protein
human ACE2
COVID-19 vaccine
mutation
infection
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