Cryo-EM reveals 2.35 Å structure of Andes hantavirus glycoprotein tetramers on virus-like particles
By
Jason S. McLellan1,4,5 Send email to [email protected]
A baker's-dozen of insight crammed into one ring.
Summary
This article presents a high-resolution cryo-electron microscopy study of Andes hantavirus (ANDV) glycoprotein tetramers, achieving a 2.35 Å resolution structure. Using a virus-like particle (VLP) system, the researchers elucidated the molecular architecture of New World hantavirus glycoproteins, including the organization of tetramers and dimers of tetramers. The study also examined acid-induced membrane fusion mechanisms and antibody-mediated neutralization through ADI-65534 Fab complexes. Immunization with repRNA encoding ANDV-VLPs was shown to elicit high neutralizing-antibody titers, providing insights that could inform vaccine and therapeutic development against severe hantavirus infections.
Key quotes
· 4 pulledNew World hantaviruses cause severe infections in humans.
Previous structural studies have advanced our understanding of hantavirus glycoprotein architecture; however, the lack of high-resolution structures of the glycoprotein tetramer and its lattice organization has limited mechanistic insights into viral assembly and entry.
This enabled the determination of a 2.35 Å resolution structure of the membrane-embedded Andes virus (ANDV) gl
Immunization with repRNA encoding ANDV-VLPs elicits high neutralizing-antibody titers.
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