Deep learning-guided selection of antibody therapies with enhanced resistance to current and prospective SARS-CoV-2 Omicron variants
Frei, L.; Gao, B.; Han, J.; Taft, J. M.; Irvine, E. B.; Weber, C. R.; Kumar, R.; Eisinger, B.; Reddy, S. T.
Show abstract
Most COVID-19 antibody therapies rely on binding the SARS-CoV-2 receptor binding domain (RBD). However, heavily mutated variants such as Omicron and its sublineages, which are characterized by an ever increasing number of mutations in the RBD, have rendered prior antibody therapies ineffective, leaving no clinically approved antibody treatments for SARS-CoV-2. Therefore, the capacity of therapeutic antibody candidates to bind and neutralize current and prospective SARS-CoV-2 variants is a critical factor for drug development. Here, we present a deep learning-guided approach to identify antibodies with enhanced resistance to SARS-CoV-2 evolution. We apply deep mutational learning (DML), a machine learning-guided protein engineering method to interrogate a massive sequence space of combinatorial RBD mutations and predict their impact on angiotensin-converting enzyme 2 (ACE2) binding and antibody escape. A high mutational distance library was constructed based on the full-length RBD of Omicron BA.1, which was experimentally screened for binding to the ACE2 receptor or neutralizing antibodies, followed by deep sequencing. The resulting data was used to train ensemble deep learning models that could accurately predict binding or escape for a panel of therapeutic antibody candidates targeting diverse RBD epitopes. Furthermore, antibody breadth was assessed by predicting binding or escape to synthetic lineages that represent millions of sequences generated using in silico evolution, revealing combinations with complementary and enhanced resistance to viral evolution. This deep learning approach may enable the design of next-generation antibody therapies that remain effective against future SARS-CoV-2 variants.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Hierarchical sequence-affinity landscapes shape the evolution of breadth in an anti-influenza receptor binding site antibody 97%
- The landscape of antibody binding affinity in SARS-CoV-2 Omicron BA.1 evolution 97%
- Identification of a conserved neutralizing epitope present on spike proteins from all highly pathogenic coronaviruses 96%
Similar papers in this journal
- Synthetic coevolution reveals adaptive mutational trajectories of neutralizing antibodies and SARS-CoV-2 96%
- Rugged fitness landscapes minimize promiscuity in the evolution of transcriptional repressors 96%
- Engineering of highly active and diverse nuclease enzymes by combining machine learning and ultra-high-throughput screening 96%
Similar papers in this journal
- Convergent antibody responses to the SARS-CoV-2 spike protein in convalescent and vaccinated individuals 96%
- Interrogation of cancer gene dependencies reveals novel paralog interactions of autosome and sexchromosome encoded genes 96%
- Crimean-Congo Hemorrhagic Fever Survivors Elicit Protective Non-Neutralizing Antibodies that Target 11 Overlapping Regions on Viral Glycoprotein GP38 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.