D. Veesler

The paper identifies a conserved antigenic supersite on the SARS-CoV-2 N-terminal domain recognized by neutralizing antibodies and shows its vulnerability to mutations in variants.

This study identifies a monoclonal antibody that broadly neutralizes multiple beta-coronaviruses by targeting a conserved epitope, providing a structural basis for designing pan-coronavirus vaccines.

The paper designs modular nanocages that assemble antibodies into precise geometries, enhancing signaling and neutralization compared to free antibodies.

This study designs SARS-CoV-2 nanoparticle vaccines that induce strong neutralizing antibodies in mice, with higher titers and lower doses than existing trimer vaccines.

This paper describes a hierarchical method to design multi-scale symmetric protein complexes using repeat proteins and helical bundles, resulting in large symmetric assemblies like an icosahedral nanocage.

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.

This paper designs a stabilized SARS-CoV-2 spike glycoprotein in the closed conformation, showing it maintains structure and antigenicity while being applicable to other beta-coronaviruses.

Nanoparticle immunogens with four seasonal influenza hemagglutinins elicit neutralizing antibodies against both the head and stem, providing broad protection against diverse influenza strains.

This paper provides a protocol for pseudotyping lentiviral particles with SARS-CoV-2 Spike protein to measure neutralizing antibody activity in a luciferase-based assay.

This study identifies and characterizes a potent neutralizing antibody, S309, against SARS-CoV-2 and related sarbecoviruses, showing its efficacy in preventing viral entry and potential for therapeutic use.

This study characterizes the structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein, showing its receptor-binding properties, furin cleavage site, and potential for cross-neutralizing antibodies.

This paper describes a method to improve particle density on cryo-EM grids through multiple rounds of sample application and blotting, enhancing structural studies of various biomolecules.