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How baculovirus polyhedra fit square pegs into round holes to robustly package viruses.

DOI: 10.1038/emboj.2009.352 DOI Help
PMID: 19959989 PMID Help

Authors: Xiaoyun Ji (Division of Structural Biology, University of Oxford) , Geoff Sutton (Division of Structural Biology, University of Oxford) , Robin Owen (Diamond Light Source) , David Stuart (Diamond Light Source) , Gwyndaf Evans (Diamond Light Source) , Danny Axford (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Embo Journal , VOL 29 (2) , PAGES 505-514

State: Published (Approved)
Published: January 2010

Abstract: Natural protein crystals (polyhedra) armour certain viruses, allowing them to survive for years under hostile conditions. We have determined the structure of polyhedra of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), revealing a highly symmetrical covalently cross-braced robust lattice, the subunits of which possess a flexible adaptor enabling this supra-molecular assembly to specifically entrap massive baculoviruses. Inter-subunit chemical switches modulate the controlled release of virus particles in the unusual high pH environment of the target insect's gut. Surprisingly, the polyhedrin subunits are more similar to picornavirus coat proteins than to the polyhedrin of cytoplasmic polyhedrosis virus (CPV). It is, therefore, remarkable that both AcMNPV and CPV polyhedra possess identical crystal lattices and crystal symmetry. This crystalline arrangement must be particularly well suited to the functional requirements of the polyhedra and has been either preserved or re-selected during evolution. The use of flexible adaptors to generate a powerful system for packaging irregular particles is characteristic of the AcMNPV polyhedrin and may provide a vehicle to sequester a wide range of objects such as biological nano-particles.

Journal Keywords: Animals; Baculoviridae; Capsid; Cell; Crystallography; X-Ray; Hydrogen-Ion; Models; Molecular; Mutation; Picornaviridae; Protein; Reoviridae; Sequence; Viral Structural Proteins

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography