T. N. Starr

This study characterizes the receptor tropism and antigenicity of a clade 3 sarbecovirus, identifying broad ACE2 usage and cross-neutralizing antibodies with implications for vaccine design.

This study uses deep mutational scans to analyze epistatic effects in SARS-CoV-2 variants XBB.1.5 and BQ.1.1, revealing ongoing epistatic drift in mutation impacts.

This study uses combinatorial DMS to analyze the genetic architecture of DNA recognition by an ancient transcription factor, showing that pairwise epistasis enables functional evolution by expanding sequence space for new specificity.

This study identifies four broad, potent monoclonal antibodies against SARS-CoV-2 spike protein that neutralize multiple variants, including Omicron and XBB.1.5, targeting conserved regions with high functional constraint.

This study tracks antibody responses six months after Omicron BA.1 breakthrough infection and finds reduced neutralizing antibodies and memory B cells, with public clones dominating and predicting new sublineages.

This study uses deep mutational scanning to analyze how mutations in the Omicron BA.1 and BA.2 RBDs affect ACE2 binding, RBD folding, and antibody escape, identifying epistatic shifts and lineage-specific changes.

The paper maps how mutations in the SARS-CoV-2 Omicron BA.1 RBD affect antibody binding affinity through systematic analysis of 32,768 genotypes against four monoclonal antibodies.

This study uses molecular fate-mapping to show that repeated immunization preferentially reuses initial B cell clones over recruiting new ones, with imprinting effects decreasing as antigenic distance increases.

This study identifies compensatory epistasis in SARS-CoV-2 Omicron BA.1 that maintains ACE2 affinity despite antibody-escape mutations.

This study designs mosaic RBD nanoparticles to elicit antibodies against conserved sarbecovirus epitopes, showing broader protection against SARS-CoV-2 variants and animal sarbecoviruses in animal models.

The paper examines the antibody response to the SARS-CoV-2 Delta variant, showing it targets class 1 and 2 epitopes more than class 3, and that mutations in these regions reduce antibody binding.

The paper analyzes epistatic shifts in SARS-CoV-2 RBD mutations across variants to understand how they influence ACE2 binding and future evolution.

The paper identifies 13 rare mutations in the Omicron S-gene that cluster in functionally important regions and likely impact Spike function, suggesting cooperative interactions that mitigate fitness costs.

The paper develops an antibody-escape calculator to estimate the antigenic effects of mutations in the SARS-CoV-2 RBD, correlating with neutralization assays and highlighting Omicron's antigenic properties.

This study identifies a broadly neutralizing antibody against sarbecoviruses that targets the ACE2 binding site and shows high resistance to escape mutations.

This study compares antibody responses to early SARS-CoV-2 isolates and the B.1.351 variant, finding shifts in immunodominance hierarchy within the spike receptor-binding domain.

This study traces the evolutionary history of ACE2 binding in sarbecoviruses, finding it is an ancestral trait that has been lost in some clades and is highly evolvable through single amino-acid mutations.

This paper designs stabilized SARS-CoV-2 RBD variants using deep mutational scanning and structure-based design, showing improved thermal stability and manufacturability for vaccine applications.

The paper compares the specificity of antibodies from the mRNA-1273 vaccine and natural infection, finding vaccine antibodies are more RBD-focused but have broader epitope coverage within the RBD.

This paper identifies a human monoclonal antibody that broadly neutralizes SARS-CoV-2 variants and zoonotic sarbecoviruses by targeting a conserved epitope on the spike protein.

This study identifies antibodies against SARS-CoV-2 that balance neutralization potency and breadth, with some showing high resistance to viral escape.

The paper maps mutations in SARS-CoV-2 spike RBD that escape binding by three antibody classes and finds that plasma escape maps closely resemble those of a single antibody class targeting site E484.

The paper maps SARS-CoV-2 RBD mutations that escape LY-CoV555 and its cocktail with LY-CoV016, identifying escape mutations in circulating variants and suggesting epitope diversification for improved antibody resilience.

This paper determines the structures of two antibodies in the AZD7442 cocktail that neutralize SARS-CoV-2 and identifies critical residues for neutralization and viral escape.

This study maps mutations in the SARS-CoV-2 RBD that affect recognition by polyclonal human serum antibodies, identifying key sites like E484 that significantly reduce neutralization.

The paper maps viral mutations in SARS-CoV-2 that escape two therapeutic antibodies, identifying escape mutations present in circulating strains.

This study maps mutations in the SARS-CoV-2 spike RBD that escape antibody recognition, revealing escape mutation patterns and enabling the design of antibody cocktails.

The paper experimentally measures the effects of all amino-acid mutations in the SARS-CoV-2 RBD on protein folding and ACE2 binding, identifying constrained regions and tolerated mutations.

The paper measures the fitness effects of historical amino acid substitutions in Hsp90 across evolutionary timescales, finding pervasive epistasis influencing sequence evolution and entrenchment.