Dawid S. Zyla

The paper determines cryo-EM structures of monoclonal antibodies bound to rabies virus glycoprotein, identifying new antigenic sites and their role in neutralization.

This study identifies neutralizing epitopes on the measles virus fusion protein by analyzing monoclonal antibodies and their structural interactions with prefusion and postfusion conformations.

This study designs and tests a stabilized full-length measles fusion protein antigen that induces strong neutralizing antibodies and protects against viral challenge in a cotton rat model.

This study identifies and characterizes human monoclonal antibodies against measles virus surface proteins, revealing their epitopes and mechanisms of neutralization.

This study determines the pre- and post-fusion structures of HERV-K Env using cryo-EM, revealing unique features that may inform therapeutic strategies.

This study presents a pre-fusion, open conformation of the SARS-CoV-2 S2 subunit and identifies antibodies that recognize it, providing insights into spike dynamics and potential vaccine targets.

This study uses cryo-electron tomography to reveal the structure of the intracellular Ebola virus nucleocapsid, identifying a new outer layer of NP complexed with VP35 and conserved assembly interfaces.

The paper presents the cryo-EM structure of the type 1 chaperone-usher pilus rod at 4.2 Å resolution, revealing its spring-like biomechanical properties.