SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Lizhou ZhangDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USACody B. JacksonDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAHuihui MouDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAAmrita OjhaDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAHaiyong PengDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USABrian D. QuinlanDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAErumbi S. RangarajanDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, USAAndi PanDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAAbigail VanderheidenDepartment of Pediatrics, Division of Infectious Disease, Emory University School of Medicine, Atlanta, GA, USAMehul S. SutharDepartment of Pediatrics, Division of Infectious Disease, Emory University School of Medicine, Atlanta, GA, USAWenhui LiNational Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, ChinaTina IzardDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, USAChristoph RaderDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USAMichael FarzanDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA. [email protected]Hyeryun ChoeDepartment of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA. [email protected]
2020en
ABI
Annotatsiya
Abstract SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S G614 ) with the original (S D614 ). We report here pseudoviruses carrying S G614 enter ACE2-expressing cells more efficiently than those with S D614 . This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results are obtained with virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, D614G does not alter S-protein binding to ACE2 or neutralization sensitivity of pseudoviruses. Thus, D614G may increase infectivity by assembling more functional S protein into the virion.
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