Integrated cryoEM structure of a spumaretrovirus reveals cross-kingdom evolutionary relationships and the molecular basis for assembly and virus entry

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

Abstract

Foamy viruses (FVs) are an ancient lineage of retroviruses, with an evolutionary history spanning over 450 million years. Vector systems based on Prototype Foamy Virus (PFV) are promising candidates for gene and oncolytic therapies. Structural studies of PFV contribute to the understanding of the mechanisms of FV replication, cell entry and infection, and retroviral evolution. Here we combine cryoEM and cryoET to determine high-resolution in situ structures of the PFV icosahedral capsid (CA) and envelope glycoprotein (Env), including its type III transmembrane anchor and membrane-proximal external region (MPER), and show how they are organized in an integrated structure of assembled PFV particles. The atomic models reveal an ancient retroviral capsid architecture and an unexpected relationship between Env and other class 1 fusion proteins of the Mononegavirales. Our results represent the de novo structure determination of an assembled retrovirus particle.

Details

OriginalspracheEnglisch
Seiten (von - bis)4213-4230.e19
FachzeitschriftCell
Jahrgang187
Ausgabenummer16
PublikationsstatusVeröffentlicht - 8 Aug. 2024
Peer-Review-StatusJa

Externe IDs

PubMed 39013471
ORCID /0000-0002-0320-4223/work/167217251

Schlagworte

Schlagwörter

  • capsid, cryo-EM, cryo-ET, foamy virus, membrane fusion, paramyxovirus, quasi-equivalence, receptor binding, retrovirus, virus evolution