Version 1
: Received: 26 March 2020 / Approved: 27 March 2020 / Online: 27 March 2020 (11:37:06 CET)
Version 2
: Received: 9 April 2020 / Approved: 9 April 2020 / Online: 9 April 2020 (09:59:37 CEST)
How to cite:
Park, Y.; Ahn, J.W.; Hwang, S.; Sung, K.S.; Lim, J.; Kwack, K. Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses. Preprints2020, 2020030409. https://doi.org/10.20944/preprints202003.0409.v2
Park, Y.; Ahn, J.W.; Hwang, S.; Sung, K.S.; Lim, J.; Kwack, K. Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses. Preprints 2020, 2020030409. https://doi.org/10.20944/preprints202003.0409.v2
Park, Y.; Ahn, J.W.; Hwang, S.; Sung, K.S.; Lim, J.; Kwack, K. Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses. Preprints2020, 2020030409. https://doi.org/10.20944/preprints202003.0409.v2
APA Style
Park, Y., Ahn, J.W., Hwang, S., Sung, K.S., Lim, J., & Kwack, K. (2020). Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses. Preprints. https://doi.org/10.20944/preprints202003.0409.v2
Chicago/Turabian Style
Park, Y., Jaejoon Lim and KyuBum Kwack. 2020 "Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses" Preprints. https://doi.org/10.20944/preprints202003.0409.v2
Abstract
Objectives Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has high infectivity in humans, attributed to the strong affinity of its spike (S) protein to human angiotensin-converting enzyme 2 (ACE2). Here, we analyzed the structural similarity of the S protein between SARS-CoV-2 and other SARS-related coronaviruses (CoVs). Methods We performed multiple alignment analysis of nine amino acid sequences of CoV S proteins from NCBI with MAFFT web-based software, followed by phylogeny analysis. Three-dimensional structure modeling was performed by SWISS-MODEL. We calculated the template modeling score between the S protein of SARS-CoV-2 and that of other SARS-related CoVs. Results The S1 domain of the unclassified CoV RaTG13 (the host of which is the intermediate horseshoe bat) was structurally very similar to that of SARS-CoV-2, implying that RaTG13 could be the origin of SARS-CoV-2. In addition, the folding property of the entire S protein was nearly the same between SARS-CoV-2 and RaTG13 after the PRRA amino acid insertion was removed from SARS-CoV-2. Conclusions RaTG13 could have a high binding affinity to ACE2, similar to SARS-CoV-2, and it is therefore highly likely to infect other animals. Therefore, massive research and monitoring of CoVs in animals is necessary to prevent future COVID-19-like disasters.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Commenter: KyuBum Kwack
Commenter's Conflict of Interests: Author