H. M. E. Duyvesteyn

This study determines the structure of NDST1, revealing its catalytic domains and a non-catalytic N-terminal domain, and proposes a mechanism for its function.

This study determines the native structure of ChAdOx1-vectored SARS-CoV-2 vaccines on cell surfaces, showing prefusion spikes in one-RBD-up conformation and improved RBD exposure in HexaPro-stabilized variants.

This study identifies a monoclonal antibody, mAb92, that targets the Nipah virus fusion glycoprotein and provides complete protection in hamsters.

This study shows that BA.4 and BA.5 variants are more resistant to neutralization by vaccine and BA.1 immune sera compared to BA.1 and BA.2.

This study identifies a viral export signal in hepatitis A virus that requires dual recruitment of HD-PTP and ALIX for nonlytic release in extracellular vesicles.

This study shows that Omicron-B.1.1.529 has extensive mutations in Spike that reduce neutralization by antibodies from vaccinated and previously infected individuals, and escape most monoclonal antibodies.

This study compares antibody resistance of SARS-CoV-2 variants P.1, B.1.351, and B.1.1.7, finding P.1 is less resistant to antibodies despite similar ACE2 binding mutations.

The paper compares glycosylation patterns of recombinant SARS-CoV-2 spike proteins across labs with infectious virus S protein, finding conserved site-specific glycan maturation stalling linked to protein structure.

This study examines how mutations in the B.1.1.7 variant of SARS-CoV-2 affect neutralization by monoclonal antibodies targeting non-RBD epitopes.

This paper identifies CR3022 as a monoclonal antibody that neutralizes SARS-CoV-2 by destroying its prefusion Spike conformation, suggesting therapeutic potential.

The paper identifies a lipid-binding pocket in the SARS-CoV-2 Spike that stabilizes the prefusion trimer and shields neutralizing epitopes, suggesting it as a potential drug target.

This paper identifies an antibody, EY6A, from a convalescent patient that neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1 by binding a conserved epitope on the Spike protein.