ArticleCommunications biology2023
Structural basis of spike RBM-specific human antibodies counteracting broad SARS-CoV-2 variants.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- CD80 (B7-1) as a potential therapeutic target in Epstein-Barr virus‑associated B cell diseases.Scientific reports · 2026Article
- The Use of Heterologous Antigens for Biopanning Enables the Selection of Broadly Neutralizing Nanobodies Against SARS-CoV-2.Antibodies (Basel, Switzerland) · 2025Article
- Structural and Functional Glycosylation of the Abdala COVID-19 Vaccine.Glycobiology · 2025Article
- Detrimental Effects of Anti-Nucleocapsid Antibodies in SARS-CoV-2 Infection, Reinfection, and the Post-Acute Sequelae of COVID-19.Pathogens (Basel, Switzerland) · 2024Review
- Article
- Two-dimensional high-throughput on-cell screening of immunoglobulins against broad antigen repertoires.Communications biology · 2024Article
Corrections and comments
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The decrease of antibody efficacy to mutated SARS-CoV-2 spike RBD explains the breakthrough infections and reinfections by Omicron variants. Here, we analyzed broadly neutralizing antibodies isolated from long-term hospitalized convalescent patients of early SARS-CoV-2 strains. One of the antibodies named NCV2SG48 is highly potent to broad SARS-CoV-2 variants including Omicron BA.1, BA.2, and BA.4/5. To reveal the mode of action, we determined the sequence and crystal structure of the Fab fragment of NCV2SG48 in a complex with spike RBD from the original, Delta, and Omicron BA.1. NCV2SG48 is from a minor V
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