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SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity

Author

Listed:
  • Lizhou Zhang

    (The Scripps Research Institute)

  • Cody B. Jackson

    (The Scripps Research Institute)

  • Huihui Mou

    (The Scripps Research Institute)

  • Amrita Ojha

    (The Scripps Research Institute)

  • Haiyong Peng

    (The Scripps Research Institute)

  • Brian D. Quinlan

    (The Scripps Research Institute)

  • Erumbi S. Rangarajan

    (The Scripps Research Institute)

  • Andi Pan

    (The Scripps Research Institute)

  • Abigail Vanderheiden

    (Division of Infectious Disease, Emory University School of Medicine
    Emory Vaccine Center, Emory University School of Medicine
    Yerkes National Primate Research Center
    Emory-UGA Center of Excellence of Influenza Research and Surveillance (CEIRS))

  • Mehul S. Suthar

    (Division of Infectious Disease, Emory University School of Medicine
    Emory Vaccine Center, Emory University School of Medicine
    Yerkes National Primate Research Center
    Emory-UGA Center of Excellence of Influenza Research and Surveillance (CEIRS))

  • Wenhui Li

    (Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University)

  • Tina Izard

    (The Scripps Research Institute)

  • Christoph Rader

    (The Scripps Research Institute)

  • Michael Farzan

    (The Scripps Research Institute)

  • Hyeryun Choe

    (The Scripps Research Institute)

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.

Suggested Citation

  • Lizhou Zhang & Cody B. Jackson & Huihui Mou & Amrita Ojha & Haiyong Peng & Brian D. Quinlan & Erumbi S. Rangarajan & Andi Pan & Abigail Vanderheiden & Mehul S. Suthar & Wenhui Li & Tina Izard & Christ, 2020. "SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19808-4
    DOI: 10.1038/s41467-020-19808-4
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    Cited by:

    1. Ren Ren & Shenglin Cai & Xiaona Fang & Xiaoyi Wang & Zheng Zhang & Micol Damiani & Charlotte Hudlerova & Annachiara Rosa & Joshua Hope & Nicola J. Cook & Peter Gorelkin & Alexander Erofeev & Pavel Nov, 2023. "Multiplexed detection of viral antigen and RNA using nanopore sensing and encoded molecular probes," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Raveen Rathnasinghe & Sonia Jangra & Chengjin Ye & Anastasija Cupic & Gagandeep Singh & Carles Martínez-Romero & Lubbertus C. F. Mulder & Thomas Kehrer & Soner Yildiz & Angela Choi & Stephen T. Yeung , 2022. "Characterization of SARS-CoV-2 Spike mutations important for infection of mice and escape from human immune sera," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Sun Jin Kim & Zhong Yao & Morgan C. Marsh & Debra M. Eckert & Michael S. Kay & Anna Lyakisheva & Maria Pasic & Aiyush Bansal & Chaim Birnboim & Prabhat Jha & Yannick Galipeau & Marc-André Langlois & J, 2022. "Homogeneous surrogate virus neutralization assay to rapidly assess neutralization activity of anti-SARS-CoV-2 antibodies," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    4. Uddhav Timilsina & Supawadee Umthong & Emily B. Ivey & Brandon Waxman & Spyridon Stavrou, 2022. "SARS-CoV-2 ORF7a potently inhibits the antiviral effect of the host factor SERINC5," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    5. Scott B. Biering & Francielle Tramontini Gomes de Sousa & Laurentia V. Tjang & Felix Pahmeier & Chi Zhu & Richard Ruan & Sophie F. Blanc & Trishna S. Patel & Caroline M. Worthington & Dustin R. Glasne, 2022. "SARS-CoV-2 Spike triggers barrier dysfunction and vascular leak via integrins and TGF-β signaling," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    6. Antoni G. Wrobel & Donald J. Benton & Chloë Roustan & Annabel Borg & Saira Hussain & Stephen R. Martin & Peter B. Rosenthal & John J. Skehel & Steven J. Gamblin, 2022. "Evolution of the SARS-CoV-2 spike protein in the human host," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    7. Alexander J. Pak & Alvin Yu & Zunlong Ke & John A. G. Briggs & Gregory A. Voth, 2022. "Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    8. Eakachai Prompetchara & Chutitorn Ketloy & Mohamad-Gabriel Alameh & Kittipan Tharakhet & Papatsara Kaewpang & Nongnaphat Yostrerat & Patrawadee Pitakpolrat & Supranee Buranapraditkun & Suwimon Manopwi, 2023. "Immunogenicity and protective efficacy of SARS-CoV-2 mRNA vaccine encoding secreted non-stabilized spike in female mice," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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