Structural impact on SARS-CoV-2 spike protein by D614G substitution
| Autor: | Sarah M. Sterling, Richard M. Walsh, Hanqin Peng, Bing Chen, Jun Zhang, Alec N. Woosley, Tianshu Xiao, Jianming Lu, Wei Yang, Sophia Rits-Volloch, Haisun Zhu, Piotr Sliz, Yongfei Cai |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Protein Conformation Protein domain Trimer Plasma protein binding Protomer Antibodies Viral Protein structure Protein Domains Viral entry Aspartic acid Humans Multidisciplinary Chemistry SARS-CoV-2 Cryoelectron Microscopy Lipid bilayer fusion COVID-19 Virus Internalization Protein Subunits Amino Acid Substitution Spike Glycoprotein Coronavirus Biophysics Mutant Proteins Angiotensin-Converting Enzyme 2 Hydrophobic and Hydrophilic Interactions Protein Binding Receptors Coronavirus |
| Zdroj: | Science (New York, N.Y.). 372(6541) |
| ISSN: | 1095-9203 |
| Popis: | How an early variant got ahead Throughout the COVID-19 pandemic, epidemiologists have monitored the evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) with particular focus on the spike protein. An early variant with an aspartic acid (D) to glycine (G) mutation at position 614, D614G, rapidly became dominant and is maintained in current variants of concern. Zhang et al. investigated the structural basis for the increased spread of this variant, which does so even though it binds less tightly to the host receptor (see the Perspective by Choe and Farzan). Structural and biochemical studies on a full-length G614 spike trimer showed that there are interactions not present in D614 that prevent premature loss of the S1 subunit that binds angiotensin-converting enzyme 2. This stabilization effectively increases the number of spikes that can facilitate infection. Science , this issue p. 525 ; see also p. 466 |
| Databáze: | OpenAIRE |
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