The N-terminal domain of spike glycoprotein mediates SARS-CoV-2 infection by associating with L-SIGN and DC-SIGN
Open accessAbstract
The widespread occurrence of SARS-CoV-2 has had a profound effect on society and a vaccine is currently being developed. Angiotensin-converting enzyme 2 (ACE2) is the primary host cell receptor that interacts with the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. Although pneumonia is the main symptom in severe cases of SARS-CoV-2 infection, the expression levels of ACE2 in the lung is low, suggesting the presence of another receptor for the spike protein. In order to identify the additional receptors for the spike protein, we screened a receptor for the SARS-CoV-2 spike protein from the lung cDNA library. We cloned L-SIGN as a specific receptor for the N-terminal domain (NTD) of the SARS-CoV-2 spike protein. The RBD of the spike protein did not bind to L-SIGN. In addition, not only L-SIGN but also DC-SIGN, a closely related C-type lectin receptor to L-SIGN, bound to the NTD of the SARS-CoV-2 spike protein. Importantly, cells expressing L-SIGN and DC-SIGN were both infected by SARS-CoV-2. Furthermore, L-SIGN and DC-SIGN induced membrane fusion by associating with the SARS-CoV-2 spike protein. Serum antibodies from infected patients and a patient-derived monoclonal antibody against NTD inhibited SARS-CoV-2 infection of L-SIGN or DC-SIGN expressing cells. Our results highlight the important role of NTD in SARS-CoV-2 dissemination through L-SIGN and DC-SIGN and the significance of having anti-NTD neutralizing antibodies in antibody-based therapeutics.
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Hierarchy of Complex Glycomacromolecules: From Controlled Topologies to Biomedical Applications
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The SARS-CoV-2 Delta variant is poised to acquire complete resistance to wild-type spike vaccinesPreprint
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LRRC15 inhibits SARS-CoV-2 cellular entry in trans
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SARS-CoV-2 spike conformation determines plasma neutralizing activityPreprint
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Chaudhari, A. M., Singh, I., Joshi, M. N., Patel, A. K., & Joshi, C. G. (2022) · Molecular Diversity · doi:10.1007/s11030-022-10405-9 · Cited by 20 · see citing works
SARS-CoV-2 spike variants differ in their allosteric responses to linoleic acid
Oliveira, A. S., Shoemark, D., Davidson, A., Berger, I., Schaffitzel, C., & Mulholland, A. (2022) · bioRxiv · doi:10.1093/jmcb/mjad021 · Cited by 14 · see citing works
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SARS-CoV-2 hijacks neutralizing dimeric IgA for nasal infection and injury in Syrian hamsters 1
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Neutralizing and enhancing antibodies against SARS-CoV-2
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Self-citationEpigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
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The seasonal behaviour of COVID-19 and its galectin-like culprit of the viral spike
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LRRC15 is an inhibitory receptor blocking SARS-CoV-2 spike-mediated entry in transPreprint
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Evolving spike-protein N -glycosylation in SARS-CoV-2 variantsPreprint
Baboo, S., Diedrich, J. K., Torres, J. L., Copps, J., Singh, B., Garrett, P. T., Ward, A. B., Paulson, J. C., & Yates, J. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.08.539897 · Cited by 11 · see citing works
SARS-CoV-2 hijacks neutralizing dimeric IgA for enhanced nasal infection and injuryPreprint
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Pathogen Genomics and Host Cellular Susceptibility Factors of COVID-19
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Glycan Epitopes and Potential Glycoside Antagonists of DC-SIGN Involved in COVID-19: In Silico Study
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SARS-CoV-2 spike variants differ in their allosteric response to linoleic acidPreprint
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Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2
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A murine model of DC-SIGN humanization exhibits increased susceptibility against SARS-CoV-2
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Research progress in Fc‐effector functions against SARS‐CoV‐2
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Genetic Architecture of Host Proteins Involved in SARS-CoV
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Syncytia Formation in the Pathogenesis of SARS-CoV-2 Infection: Lessons from Viral Infections
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- Authors
- Soh, W. T., Liu, Y., Nakayama, E. E., Ono, C., Torii, S., Nakagami, H., Matsuura, Y., Shioda, T., & Arase, H.
- Affiliations
- The University of Osaka (JP)
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- Corresponding author
- Arase, Hisashi
- ORCID
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2020-11-05
- OpenAlex
- W3097426086
- Semantic Scholar
- bb3127eb654e9aa3fc55a2d7169c69ebff3adb8e
- Cited by
- 61
- References
- 46
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 5 · 2023: 6 · 2022: 15 · 2021: 30 · 2020: 3
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- Japan Agency for Medical Research and Development (19fk0108161h0001)
- Kishimoto Foundation
- Ministry of Education, Culture, Sports, Science and Technology (JP18H05279, JP19H04808)
- Japan Society for the Promotion of Science (18H05279, 19H03478)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, spike protein, N-terminal domain, L-SIGN, DC-SIGN, C-type lectin receptors, viral entry receptor, membrane fusion, neutralizing antibodies, monoclonal antibodies, pulmonary infection, therapeutic antibodies
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