ArticleNature communications2024
Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Structural polymorphism of two-dimensional lattices assembled from baculoviral capsid proteins.Virologica Sinica · 2025Article
- Baculovirus 25K hijacks host UAP56 to facilitate nuclear export of viral mRNA in insect cells.Journal of virology · 2025Article
- Fungal Pathogen Infection byBiology · 2025Article
- Regulation ofViruses · 2025Review
- Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus.Nature communications · 2025Article
- The nucleocapsid architecture and structural atlas of the prototype baculovirus define the hallmarks of a new viral realm.Science advances · 2024Article
- The conserved cysteines at position 18, 36, and 49 of Autographa californica multiple nucleopolyhedrovirus VP39 are essential for virus replication.Virus genes · 2024Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Architecture of the baculovirus nucleocapsid revealed by cryo-EM.Nature communications · 2023Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
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.
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