Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly

Friederike M.C. Benning; Simon Jenni; Coby Y. Garcia; Tran H. Nguyen; Xuewu Zhang; Luke H. Chao

doi:10.1038/s41467-023-44596-y

Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly

Friederike M.C. Benning, Simon Jenni, Coby Y. Garcia, Tran H. Nguyen, Xuewu Zhang, Luke H. Chao

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

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.

Original language	English (US)
Article number	250
Journal	Nature communications
Volume	15
Issue number	1
DOIs	https://doi.org/10.1038/s41467-023-44596-y
State	Published - Dec 2024

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

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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 {\AA} 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.",

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AU - Benning, Friederike M.C.

AU - Jenni, Simon

AU - Garcia, Coby Y.

AU - Nguyen, Tran H.

AU - Zhang, Xuewu

AU - Chao, Luke H.

PY - 2024/12

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Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly

Abstract

ASJC Scopus subject areas

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