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SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity.
Zhang, Lizhou; Jackson, Cody B; Mou, Huihui; Ojha, Amrita; Peng, Haiyong; Quinlan, Brian D; Rangarajan, Erumbi S; Pan, Andi; Vanderheiden, Abigail; Suthar, Mehul S; Li, Wenhui; Izard, Tina; Rader, Christoph; Farzan, Michael; Choe, Hyeryun.
  • Zhang L; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Jackson CB; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Mou H; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Ojha A; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Peng H; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Quinlan BD; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Rangarajan ES; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL, USA.
  • Pan A; Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
  • Vanderheiden A; Department of Pediatrics, Division of Infectious Disease, Emory University School of Medicine, Atlanta, GA, USA.
  • Suthar MS; Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, USA.
  • Li W; Yerkes National Primate Research Center, Atlanta, GA, USA.
  • Izard T; Emory-UGA Center of Excellence of Influenza Research and Surveillance (CEIRS), Atlanta, GA, USA.
  • Rader C; Department of Pediatrics, Division of Infectious Disease, Emory University School of Medicine, Atlanta, GA, USA.
  • Farzan M; Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, USA.
  • Choe H; Yerkes National Primate Research Center, Atlanta, GA, USA.
Nat Commun ; 11(1): 6013, 2020 11 26.
Article in English | MEDLINE | ID: covidwho-947533
ABSTRACT
SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (SG614) with the original (SD614). We report here pseudoviruses carrying SG614 enter ACE2-expressing cells more efficiently than those with SD614. 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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Full text: Available Collection: International databases Database: MEDLINE Main subject: Virion / Virus Assembly / Virus Internalization / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Observational study Topics: Variants Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2020 Document Type: Article Affiliation country: S41467-020-19808-4

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Virion / Virus Assembly / Virus Internalization / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Observational study Topics: Variants Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2020 Document Type: Article Affiliation country: S41467-020-19808-4