Antibody‐mediated SARS‐CoV‐2 entry in cultured cells

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 th...

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Bibliographic Details
Published in:EMBO reports 2023-12, Vol.24 (12), p.e57724-n/a
Main Authors: Kibria, Md Golam, Lavine, Christy L, Tang, Weichun, Wang, Shaowei, Gao, Hailong, Shi, Wei, Zhu, Haisun, Voyer, Jewel, Rits‐Volloch, Sophia, Keerti, Bi, Caihong, Peng, Hanqin, Wesemann, Duane R, Lu, Jianming, Xie, Hang, Seaman, Michael S, Chen, Bing
Format: Article
Language:English
Subjects:
ACE2
Angiotensin
Angiotensin-Converting Enzyme 2
Antibodies
antibody
Binding
Carrier Proteins - metabolism
Cell culture
Cell membranes
Cells, Cultured
Chimeras
Coronaviruses
COVID-19
Fc receptors
Fusion protein
Humans
IgG antibody
Immune response
Immunoglobulin G
Infectivity
Membrane fusion
Membranes
Monoclonal antibodies
Neutralizing
Pathogenesis
Pathogenicity
Peptidyl-dipeptidase A
Protein Binding
Proteins
receptor
Receptors
SARS-CoV-2
Severe acute respiratory syndrome
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - genetics
Spike protein
Tropism
Viral diseases
viral entry
Viruses
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Summary: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. Synopsis SARS‐CoV‐2 enters host cells by first engaging its cellular receptor to induce membrane fusion. Certain monoclonal neutralizing antibodies can independently function as a receptor to support viral infectivity in cultured cells. Monoclonal neutralizing antibodies can serve as an entry receptor for SARS‐CoV‐2 in cell culture. Receptor‐like antibodies can function in three different membrane‐bound forms. The cognate receptor ACE2 is dispensable for SARS‐CoV‐2 entry in vitro. SARS‐CoV‐2 enters host cells by first engaging its cellular receptor to induce membrane fusion. Certain monoclonal neutralizing antibodies can independently function as a receptor to support viral infectivity in cultured cells.
ISSN:1469-221X
1469-3178
DOI:10.15252/embr.202357724