Novel asymmetric isopeptide bond steers directional genomic RNA egress from icosahedral virus

ABSTRACT: How essential asymmetries are built into icosahedral virus to facilitate directional genome egress is unknown. Here we capture the structure and dynamics of disassembly intermediates of an icosahedral virus. We reveal localized RNA density poised for release beneath 5-fold axes on one half of the viral particle. The asymmetric distribution of RNA is associated with a unique interchain isopeptide bond (Glu-Lys) that flanks RNA interacting loci on the capsid protein N-terminus. This singular isopeptide bond confers an essential 'loaded-die' feature that steers directional genome egress into target host cells.

INSTRUMENT(S):

ORGANISM(S): Turnip Crinkle Virus

TISSUE(S): Leaf

SUBMITTER: Sean Braet  

LAB HEAD: Ganesh S. Anand

PROVIDER: PXD067878 | Pride | 2025-11-06

REPOSITORIES: Pride