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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/4598
RBD mutations from circulating SARS-CoV-2 strains enhance the structure stability and infectivity of the spike protein | |
Junxian Ou. Zhonghua Zhou. Ruixue Dai. Jing Zhang. Wendong Lan. Shan Zhao. Jianguo Wu. Donald Seto. Lilian Cui. Gong Zhang. Qiwei Zhang. | |
Acceso Abierto | |
Atribución-NoComercial-SinDerivadas | |
10.1101/2020.03.15.991844 | |
Spike protein receptor binding domain (RBD) of SARS-CoV-2 is the critical determinant of viral tropism and infectivity. Genomes of global SARS-CoV-2 strains were analyzed, yielding 32 RBD mutant strains clustering into 10 mutation types under high positive selection pressure. Three mutation types circulating in Wuhan, Shenzhen, Hong Kong, and France, displayed enhanced structural stability along with higher human ACE2 receptor affinity of the spike protein, indicating these mutants may have acquired increased infectivity to humans. | |
www.biorxiv.org | |
2020 | |
Artículo | |
https://www.biorxiv.org/content/10.1101/2020.03.15.991844v4.full.pdf | |
Inglés | |
VIRUS RESPIRATORIOS | |
Aparece en las colecciones: | Artículos científicos |
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