8TAF

Autographa californica multiple nucleopolyhedrovirus VP39

Summary for 8TAF

• Entry DOI: 10.2210/pdb8taf/pdb
• EMDB information: 41133
• Descriptor: Major viral capsid protein, ZINC ION (2 entities in total)
• Functional Keywords: nucleocapsid protein vp39, viral protein
• Biological source: Autographa californica multiple nucleopolyhedrovirus
• Total number of polymer chains: 8
• Total formula weight: 286870.65

Authors

Benning, F.M.C.,Chao, L.H. (deposition date: 2023-06-27, release date: 2024-01-10, Last modification date: 2025-05-28)

Primary citation

Benning, F.M.C.,Jenni, S.,Garcia, C.Y.,Nguyen, T.H.,Zhang, X.,Chao, L.H.
Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly.
Nat Commun, 15:250-250, 2024

PubMed Abstract: Baculoviruses are insect-infecting pathogens with wide applications as biological pesticides, in vitro protein production vehicles and gene therapy tools. Its cylindrical nucleocapsid, which encapsulates and protects the circular double-stranded viral DNA encoding proteins for viral replication and entry, is formed by the highly conserved major capsid protein VP39. The mechanism for VP39 assembly remains unknown. We use electron cryomicroscopy to determine a 3.2 Å helical reconstruction of an infectious nucleocapsid of Autographa californica multiple nucleopolyhedrovirus, revealing how dimers of VP39 assemble into a 14-stranded helical tube. We show that VP39 comprises a distinct protein fold conserved across baculoviruses, which includes a Zinc finger domain and a stabilizing intra-dimer sling. Analysis of sample polymorphism shows that VP39 assembles in several closely-related helical geometries. This VP39 reconstruction reveals general principles for baculoviral nucleocapsid assembly.

PubMed: 38177118
DOI: 10.1038/s41467-023-44596-y

Experimental method

ELECTRON MICROSCOPY (3.2 Å)