ArticleJournal of virology2010
Specificity of baculovirus P6.9 basic DNA-binding proteins and critical role of the C terminus in virion formation.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 55 citations in OpenAlex.
- Phosphorylation of the protamine-like protein from baculovirus affects its DNA binding and virus propagation.Nucleic acids research · 2025Article
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- Transcriptional dynamics during Heliothis zea nudivirus 1 infection in an ovarian cell line fromThe Journal of general virology · 2025Article
- Characterisation of extracellular vesicles in baculovirus infection ofJournal of extracellular biology · 2024Article
- Comparative genomics of the Neodiprion sertifer nucleopolyhedrovirus from Turkey with the fewest ORFs among baculoviruses.Virus genes · 2024Article
- Multifaceted interactions between host ESCRT-III and budded virus-related proteins involved in entry and egress of the baculovirus Autographa californica multiple nucleopolyhedrovirus.Journal of virology · 2024Article
- Functional characterization ofJournal of virology · 2023Article
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- Label-free proteomics analysis on the envelope of budded viruses of Bombyx mori nucleopolyhedrovirus harboring differential localized GP64.Virus genes · 2023Article
- Bombyx mori Nucleopolyhedrovirus Hijacks Multivesicular Body as an Alternative Envelopment Platform for Budded Virus Egress.Journal of virology · 2023Article
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- Successful Rescue of Synthetic AcMNPV with a ~17 kb Deletion in the C1 Region of the Genome.Viruses · 2022Article
- A Renewed Appreciation ofViruses · 2022Article
- Identification and Full Characterisation of Two Novel Crustacean Infecting Members of the FamilyViruses · 2021Article
- Systematic Analysis of 42 Autographa Californica Multiple Nucleopolyhedrovirus Genes Identifies An Additional Six Genes Involved in the Production of Infectious Budded Virus.Virologica Sinica · 2021Article
- VP39 of Spodoptera litura multicapsid nucleopolyhedrovirus cannot efficiently rescue the nucleocapsid assembly of vp39-null Autographa californica multiple nucleopolyhedrovirus.Virology journal · 2021Article
- Nucleocapsid Assembly of Baculoviruses.Viruses · 2019Review
- Baculovirus-Encoded MicroRNAs: A Brief Overview and Future Prospects.Current microbiology · 2019Review
- The Autographa californica Multiple NucleopolyhedrovirusJournal of virology · 2019Article
- Ascovirus P64 Homologs: A Novel Family of Large Cationic Proteins That Condense Viral Genomic DNA for Encapsidation.Biology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of double-stranded DNA (dsDNA) viruses infecting eukaryotic organisms use host- or virus-expressed histones or protamine-like proteins to condense their genomes. In contrast, members of the Baculoviridae family use a protamine-like protein named P6.9. The dephosphorylated form of P6.9 binds to DNA in a non-sequence-specific manner. By using a p6.9-null mutant of Autographa californica multiple nucleopolyhedrovirus (AcMNPV), we demonstrate that P6.9 is not required for viral DNA replication but is essential for the production of infectious virus. Virion production was rescued by P6.9 homologs from a number of Alphabaculovirus species and one Gammabaculovirus species but not from the genus Betabaculovirus, comprising the granuloviruses, or by the P6.9 homolog VP15 from the unrelated white spot syndrome virus of shrimp. Mutational analyses demonstrated that AcMNPV P6.9 with a conserved 11-residue deletion of the C terminus was not capable of rescuing p6.9-null AcMNPV, while a chimeric Betabaculovirus P6.9 containing the P6.9 C-terminal region of an Alphabaculovirus strain was able to do so. This implies that the C terminus of baculovirus P6.9 contains sequence elements essential for virion formation. Such elements may possibly interact with species- or genus-specific domains of other nucleocapsid proteins during virus assembly.
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