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TitleHigh-resolution in situ structures of hantavirus glycoprotein tetramers.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJun 18, 2025
AuthorsLuqiang Guo / Elizabeth McFadden / Megan M Slough / E Taylor Stone / Jacob Berrigan / Eva Mittler / Kiara Hatzakis / Troy Hinkley / Heather S Kain / Zunlong Ke / Nikole L Warner / Jesse H Erasmus / Kartik Chandran / Jason S McLellan /
PubMed AbstractNew World hantaviruses cause severe infections in humans, with case fatality rates approaching 40%. Previous structural studies have advanced our understanding of hantavirus glycoprotein architecture ...New World hantaviruses cause severe infections in humans, with case fatality rates approaching 40%. Previous structural studies have advanced our understanding of hantavirus glycoprotein architecture and function, however, the lack of high-resolution in situ structures of the glycoprotein tetramer and its lattice organization has limited mechanistic insights into viral assembly, entry, and antigenicity. Here, we leveraged a virus-like particle (VLP) system to establish a cryo-electron microscopy workflow for lattice-forming viral glycoproteins. This enabled the determination of a 2.35 Å resolution structure of the membrane-embedded Andes virus (ANDV) glycoprotein tetramer, as well as structures of dimers of tetramers and a complex with antibody ADI-65534. These structures reveal previously uncharacterized features of glycoprotein organization, stability, and pH-sensing. Immunization of mice with self-amplifying replicon RNA (repRNA) encoding ANDV-VLPs elicited high levels of glycoprotein-binding antibodies but equivalent titers of neutralizing antibodies compared to repRNA-encoded native ANDV glycoprotein complex. Collectively, these findings advance our understanding of hantavirus glycoprotein assemblies and their function, laying a foundation for structure-based vaccine design efforts.
External linksbioRxiv / PubMed:40667040 / PubMed Central
MethodsEM (single particle)
Resolution2.35 - 6.8 Å
Structure data

71241

9p3i

EMDB-71241, PDB-9p3i:
High-resolution in situ ANDV single tetramer structure
Method: EM (single particle) / Resolution: 2.35 Å

71242

9p3l

EMDB-71242, PDB-9p3l:
Structure of ANDV dimer of tetramer at conformation III
Method: EM (single particle) / Resolution: 3.37 Å

71243

9p3m

EMDB-71243, PDB-9p3m:
Structure of the ANDV dimer of tetramer at conformation II
Method: EM (single particle) / Resolution: 3.43 Å

71258

9p3x

EMDB-71258, PDB-9p3x:
Structure of the ANDV dimer of tetramer at conformation I
Method: EM (single particle) / Resolution: 3.18 Å

71259

9p3y

EMDB-71259, PDB-9p3y:
Andes virus glycoprotein tetramer in complex with ADI-65534 Fab
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-71260: ADI-65534-bound dimer of ANDV glycoprotein tetramers
Method: EM (single particle) / Resolution: 6.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • orthohantavirus andesense
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / hantavirus / ANDV / viral glycoprotein / tetramer / hantavirus glycoprotein / dimer of tetramer / Gn and Gc / Gn-Gc / VIRAL PROTEIN/IMMUNE SYSTEM / Gn/Gc / prefusion / antibody / neutralizing / quaternary epitope / VIRAL PROTEIN-IMMUNE SYSTEM complex

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