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TitleHelical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 250, Year 2024
Publish dateJan 4, 2024
AuthorsFriederike M C Benning / Simon Jenni / Coby Y Garcia / Tran H Nguyen / Xuewu Zhang / Luke H Chao /
PubMed AbstractBaculoviruses are insect-infecting pathogens with wide applications as biological pesticides, in vitro protein production vehicles and gene therapy tools. Its cylindrical nucleocapsid, which ...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.
External linksNat Commun / PubMed:38177118 / PubMed Central
MethodsEM (helical sym.)
Resolution3.2 Å
Structure data

41133

8taf

EMDB-41133, PDB-8taf:
Autographa californica multiple nucleopolyhedrovirus VP39
Method: EM (helical sym.) / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • autographa californica multiple nucleopolyhedrovirus
KeywordsVIRAL PROTEIN / nucleocapsid protein VP39

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