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PreprintCited by 4Viral Infectious Diseases and Gene Expression in InsectsAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

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Structure of AcMNPV nucleocapsid reveals DNA portal organization and packaging apparatus of circular dsDNA baculovirus

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Effantin, Gregory, Kandiah, Eaazhisai, Pelosse, Martin·2024·Nature Communications
DOI 10.1101/2024.10.25.620294PMC PMC12103608

Preprint — published as 10.1038/s41467-025-60152-2 · Paper page

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Abstract

Baculoviruses are large DNA viruses found in nature propagating amongst insects and lepidoptera in particular. Their viral cycle has been studied and characterized over decades and they are nowadays considered as invaluable biotechnology tools widely used as biopesticides, recombinant expression systems or delivery vehicle for gene therapy. However, very little is known about the baculovirus nucleocapsid assembly at a molecular level. Here, we solved the whole structure of the nucleocapsid of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) by applying cryo-electron microscopy (CryoEM) combined to de novo modelling and Alphafold2 predictions. Our structure completes prior observations from the helical sheath and the basal structure and elucidate the intricate architecture of the apical cap, unravelling for the first time the organization of a baculoviral DNA portal featuring intriguing symmetry mismatches between its core and vertex. The core, closing the capsid at the apex, holds two antiparallel DNA helices of the covalently closed circular (ccc) DNA genome tethered to Ac54 proteins. Different symmetry components at the apical cap and basal structure are constituted of the same building block, made of Ac101/Ac144, proving the versatility of this modular pair. The crown forming the portal vertex displays a C21 symmetry and contains, amongst others, the motor-like protein Ac66. Our findings support the viral portal to be involved in DNA packaging, most probably in conjunction with other parts of a larger DNA packaging apparatus that are not bound to mature virions and await further elucidation.

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Metadata

Authors
Effantin, G., Kandiah, E., & Pelosse, M.
Affiliations
  • European Synchrotron Radiation Facility (FR)
  • European Molecular Biology Laboratory (FR)
Corresponding author
  • Kandiah, Eaazhisai
  • Pelosse, Martin
ORCID
Venue
Nature Communications
Publisher
openRxiv
Published
2024-10-25
Volume
16
Issue
1
Pages
4844-4844
ISSN
2041-1723 (ISSN-L)
DOI
10.1101/2024.10.25.620294
PMC
PMC12103608
OpenAlex
W4410707185
Cited by
4
References
1
Citations by year
2025: 4
FWCI
1.20
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
European Synchrotron Radiation Facility
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
Autographa californica nuclear polyhedrosis virus, capsid structure, apical cap, symmetry mismatch
MeSH terms
Animals, Capsid, DNA, Circular, DNA, Viral, Models, Molecular, Genome, Viral, Nucleopolyhedroviruses, Spodoptera, Virus Assembly, Nucleocapsid, Cryoelectron Microscopy, Capsid Proteins, Sf9 Cells

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