ArticleFrontiers in immunology2022
Antigenic Cross-Reactivity Between SARS-CoV-2 S1-RBD and Its Receptor ACE2.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Angiotensin-Converting Enzyme-2 (ACE2) Downregulation During Coronavirus Infection.Molecular biotechnology · 2025Review
- Autoantibodies targeting angiotensin-converting enzyme 2 are prevalent and not induced by SARS-CoV-2 infection.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Sequential SARS-CoV-2 mRNA Vaccination Induces Anti-Idiotype (Anti-ACE2) Antibodies in K18 Human ACE2 Transgenic Mice.Vaccines · 2025Article
- The past, present, and future of anti-idiotype antibodies.Frontiers in immunology · 2025Article
- Autoantibodies Targeting G-Protein-Coupled Receptors and RAS-Related Molecules in Post-Acute COVID Vaccination Syndrome: A Retrospective Case Series Study.Biomedicines · 2024Article
- Enhancement of NETosis by ACE2-cross-reactive anti-SARS-CoV-2 RBD antibodies in patients with COVID-19.Journal of biomedical science · 2024Article
- The immunobiology of SARS-CoV-2 infection and vaccine responses: potential influences of cross-reactive memory responses and aging on efficacy and off-target effects.Frontiers in immunology · 2024Review
- Autoantibodies in COVID-19: implications for disease severity and clinical outcomes.Frontiers in immunology · 2024Review
- SARS-CoV-2 and Its Bacterial Co- or Super-Infections Synergize to Trigger COVID-19 Autoimmune Cardiopathies.International journal of molecular sciences · 2023Article
- Solved the enigma of pediatric severe acute hepatitis of unknown origin?Frontiers in cellular and infection microbiology · 2023Review
- Shared 6mer Peptides of Human and Omicron (21K and 21L) at SARS-CoV-2 Mutation Sites.Antibodies (Basel, Switzerland) · 2022Article
- Severe acute hepatitis in children with unknown aetiology, etiology analysis and the next action.Virologica Sinica · 2022Article
- Antibodies against the SARS-CoV-2 S1-RBD cross-react with dengue virus and hinder dengue pathogenesis.Frontiers in immunology · 2022Article
- Serological responses triggered by different SARS-CoV-2 vaccines against SARS-CoV-2 variants in Taiwan.Frontiers in immunology · 2022Article
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Authors and funding
19 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an emerging virus responsible for the ongoing COVID-19 pandemic. SARS-CoV-2 binds to the human cell receptor angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain in the S1 subunit of the spike protein (S1-RBD). The serum levels of autoantibodies against ACE2 are significantly higher in patients with COVID-19 than in controls and are associated with disease severity. However, the mechanisms through which these anti-ACE2 antibodies are induced during SARS-CoV-2 infection are unclear. In this study, we confirmed the increase in antibodies against ACE2 in patients with COVID-19 and found a positive correlation between the amounts of antibodies against ACE2 and S1-RBD. Moreover, antibody binding to ACE2 was significantly decreased in the sera of some COVID-19 patients after preadsorption of the sera with S1-RBD, which indicated that antibodies against S1-RBD can cross-react with ACE2. To confirm this possibility, two monoclonal antibodies (mAbs 127 and 150) which could bind to both S1-RBD and ACE2 were isolated from S1-RBD-immunized mice. Measurement of the binding affinities by Biacore showed these two mAbs bind to ACE2 much weaker than binding to S1-RBD. Epitope mapping using synthetic overlapping peptides and hydrogen deuterium exchange mass spectrometry (HDX-MS) revealed that the amino acid residues P463, F464, E465, R466, D467 and E471 of S1-RBD are critical for the recognition by mAbs 127 and 150. In addition, Western blotting analysis showed that these mAbs could recognize ACE2 only in native but not denatured form, indicating the ACE2 epitopes recognized by these mAbs were conformation-dependent. The protein-protein interaction between ACE2 and the higher affinity mAb 127 was analyzed by HDX-MS and visualized by negative-stain transmission electron microscopy imaging combined with antigen-antibody docking. Together, our results suggest that ACE2-cross-reactive anti-S1-RBD antibodies can be induced during SARS-CoV-2 infection due to potential antigenic cross-reactivity between S1-RBD and its receptor ACE2.
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