tetano
Editor, Senior Moderator
EMBO Rep
. 2023 Dec 6;24(12):e57724.
doi: 10.15252/embr.202357724. Epub 2023 Nov 2. Antibody-mediated SARS-CoV-2 entry in cultured cells
Md Golam Kibria[SUP] 1 2 [/SUP], Christy L Lavine[SUP] 3 [/SUP], Weichun Tang[SUP] 4 [/SUP], Shaowei Wang[SUP] 5 [/SUP], Hailong Gao[SUP] 1 2 [/SUP], Wei Shi[SUP] 1 2 [/SUP], Haisun Zhu[SUP] 6 [/SUP], Jewel Voyer[SUP] 1 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Keerti[SUP] 7 [/SUP], Caihong Bi[SUP] 7 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Duane R Wesemann[SUP] 7 [/SUP], Jianming Lu[SUP] 5 8 [/SUP], Hang Xie[SUP] 4 [/SUP], Michael S Seaman[SUP] 3 [/SUP], Bing Chen[SUP] 1 2 [/SUP]
Affiliations
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.
Keywords: SARS-CoV-2; antibody; receptor; viral entry.
. 2023 Dec 6;24(12):e57724.
doi: 10.15252/embr.202357724. Epub 2023 Nov 2. Antibody-mediated SARS-CoV-2 entry in cultured cells
Md Golam Kibria[SUP] 1 2 [/SUP], Christy L Lavine[SUP] 3 [/SUP], Weichun Tang[SUP] 4 [/SUP], Shaowei Wang[SUP] 5 [/SUP], Hailong Gao[SUP] 1 2 [/SUP], Wei Shi[SUP] 1 2 [/SUP], Haisun Zhu[SUP] 6 [/SUP], Jewel Voyer[SUP] 1 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Keerti[SUP] 7 [/SUP], Caihong Bi[SUP] 7 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Duane R Wesemann[SUP] 7 [/SUP], Jianming Lu[SUP] 5 8 [/SUP], Hang Xie[SUP] 4 [/SUP], Michael S Seaman[SUP] 3 [/SUP], Bing Chen[SUP] 1 2 [/SUP]
Affiliations
- PMID: 38277394
- PMCID: PMC10702815 (available on 2024-11-02)
- DOI: 10.15252/embr.202357724
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.
Keywords: SARS-CoV-2; antibody; receptor; viral entry.