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COVID-19 dominant D614G mutation in the SARS-CoV-2 spike protein desensitizes its temperature-dependent denaturation

View ORCID ProfileTzu-Jing Yang, View ORCID ProfilePei-Yu Yu, View ORCID ProfileYuan-Chih Chang, Chu-Wei Kuo, View ORCID ProfileKay-Hooi Khoo, View ORCID ProfileShang-Te Danny Hsu
doi: https://doi.org/10.1101/2021.03.28.437426
Tzu-Jing Yang
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
2Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan
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  • ORCID record for Tzu-Jing Yang
Pei-Yu Yu
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
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Yuan-Chih Chang
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
3Academia Sinica Cryo-EM Center, Academia Sinica, Taipei 11529, Taiwan
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Chu-Wei Kuo
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
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Kay-Hooi Khoo
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
2Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan
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Shang-Te Danny Hsu
1Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan
2Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan
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  • For correspondence: sthsu@gate.sinica.edu.tw
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Abstract

The D614G mutation in the spike protein of SARS-CoV-2 alters the fitness of the virus, making it the dominant form in the COVID-19 pandemic. Here we demonstrated by cryo-electron microscopy that the D614G mutation does not significantly perturb the structure of the spike protein, but multiple receptor binding domains are in an upward conformation poised for host receptor binding. The impact of the mutation lies in its ability to eliminate the unusual cold-induced unfolding characteristics, and to significantly increase the thermal stability under physiological pH. Our findings shed light on how the D614G mutation enhances the infectivity of SARS-CoV-2 through a stabilizing mutation, and suggest an approach for better design of spike-protein based conjugates for vaccine development.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted March 29, 2021.
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COVID-19 dominant D614G mutation in the SARS-CoV-2 spike protein desensitizes its temperature-dependent denaturation
Tzu-Jing Yang, Pei-Yu Yu, Yuan-Chih Chang, Chu-Wei Kuo, Kay-Hooi Khoo, Shang-Te Danny Hsu
bioRxiv 2021.03.28.437426; doi: https://doi.org/10.1101/2021.03.28.437426
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COVID-19 dominant D614G mutation in the SARS-CoV-2 spike protein desensitizes its temperature-dependent denaturation
Tzu-Jing Yang, Pei-Yu Yu, Yuan-Chih Chang, Chu-Wei Kuo, Kay-Hooi Khoo, Shang-Te Danny Hsu
bioRxiv 2021.03.28.437426; doi: https://doi.org/10.1101/2021.03.28.437426

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