OmniVira

Antibody-mediated SARS-CoV-2 entry in cultured cells.

Md Golam Kibria1,2 Christy L Lavine3 Weichun Tang4 Shaowei Wang5 Hailong Gao1,2 Wei Shi1,2 Haisun Zhu6 Jewel Voyer1 Sophia Rits-Volloch1 Keerti7 Caihong Bi7 Hanqin Peng1 Duane R Wesemann7 Jianming Lu5,8 Hang Xie4 Michael S Seaman3 Bing Chen1,2
Affiliations 8 institutions
  1. Division of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
  2. Department of Pediatrics, Harvard Medical School, Boston, MA, USA.
  3. Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA, USA.
  4. Laboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Office of Vaccines Research and Review, Center for Biologics Evaluation and Research, United States Food and Drug Administration, Silver Spring, MD, USA.
  5. Codex BioSolutions, Inc., Rockville, MD, USA.
  6. Institute for Protein Innovation, Harvard Institutes of Medicine, Boston, MA, USA.
  7. Division of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital, Ragon Institute of MGH, MIT and Harvard, Boston, MA, USA.
  8. Department of Biochemistry and Molecular and Cellular Biology, Georgetown University, Washington, DC, USA.
PMID38277394 DOI10.15252/embr.202357724 Year2023 Journal EMBO reports EMBO Rep Languageeng Statusppublish

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) enters host cells by first engaging its cellular receptor angiotensin converting enzyme 2 (ACE2) to induce conformational changes in the virus-encoded spike protein and fusion between the viral and target cell membranes. Here, we report that certain monoclonal neutralizing antibodies against distinct epitopic regions of the receptor-binding domain of the spike can replace ACE2 to serve as a receptor and efficiently support membrane fusion and viral infectivity in vitro. These receptor-like antibodies can function in the form of a complex of their soluble immunoglobulin G with Fc-gamma receptor I, a chimera of their antigen-binding fragment with the transmembrane domain of ACE2 or a membrane-bound B cell receptor, indicating that ACE2 and its specific interaction with the spike protein are dispensable for SARS-CoV-2 entry. These results suggest that antibody responses against SARS-CoV-2 may help expand the viral tropism to otherwise nonpermissive cell types with potential implications for viral transmission and pathogenesis.

antibody 9 receptor 18 SARS-CoV-2 550 viral entry 9 COVID-19 425 SARS-CoV-2 453 Angiotensin-Converting Enzyme 2 177 Carrier Proteins 4 Cells, Cultured 26 Humans 1440 Protein Binding 193 Spike Glycoprotein, Coronavirus 274 spike protein, SARS-CoV-2 157

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