ArticleCell reports2022
A key F27I substitution within HCDR1 facilitates the rapid maturation of P2C-1F11-like neutralizing antibodies in a SARS-CoV-2-infected donor.
Article in Cell reports, 2022. 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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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Affinity maturation and light-chain-mediated paratope diversification anticipates viral evolution.Cell reports · 2026Article
- Germinal center-mediated broadening of B cell responses to SARS-CoV-2 booster immunization.Science immunology · 2025Article
- RESP2: An Uncertainty Aware Multi-Target Multi-Property Optimization AI Pipeline for Antibody Discovery.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Defining a highly conserved B cell epitope in the receptor binding motif of SARS-CoV-2 spike glycoprotein.bioRxiv : the preprint server for biology · 2024Article
- Deep immunoglobulin repertoire sequencing depicts a comprehensive atlas of spike-specific antibody lineages shared among COVID-19 convalescents.Emerging microbes & infections · 2024Article
- Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies.Cell reports. Medicine · 2024Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although thousands of anti-SARS-CoV-2 monoclonal neutralizing antibodies (nAbs) have been identified and well characterized, some crucial events in the development of these nAbs during viral infection remain unclear. Using deep sequencing, we explore the dynamics of antibody repertoire in a SARS-CoV-2-infected donor, from whom the potent and broad nAb P2C-1F11 (the parent version of Brii-196) was previously isolated. Further analysis shows a rapid clonal expansion of some SARS-CoV-2-specific antibodies in early infection. Longitudinal tracing of P2C-1F11 lineage antibodies reveals that these elite nAbs were rare. Using sequence alignment, structure modeling, and bioactivity analysis based on site-mutated assay, we demonstrate that a key substitution F27I in heavy chain contributes significantly to the maturation of P2C-1F11-like antibodies. Overall, our findings elucidate the developmental process and maturation pathway of P2C-1F11, providing some important information for the design of novel immunogens to elicit more potent nAbs against SARS-CoV-2 infection.
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