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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/1779| Structural Similarity Analysis of Spike Proteins of SARS-CoV-2 and Other SARS-related Coronaviruses | |
| Park YoungJoon. Ahn Ju Won. Hwang Sojung. Sung Kyoung Su. Lim Jaejoon. Kwack KyuBum. | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| 10.20944/preprints202003.0409.v2 | |
| 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. | |
| www.preprints.org | |
| 2020 | |
| Artículo | |
| https://www.preprints.org/manuscript/202003.0409/v2/download | |
| Inglés | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Artículos científicos |
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