ArticleBMC veterinary research2018
Characterization of the DNA binding activity of structural protein VP1 from chicken anaemia virus.
Article in BMC veterinary research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A Recombinant Subunit Vaccine Against Chicken Infectious Anemia Virus Elicits Protective Immunity via VP2-Assisted VP1 Refolding.Vaccines · 2026Article
- Epidemiological Characteristics and Genetic Diversity of Chicken Infectious Anemia Virus (CIAV) in Guangdong Province, China.Veterinary sciences · 2025Article
- Recombinant Marek's disease virus expressing VP1 and VP2 proteins provides robust immune protection against chicken infectious anemia virus.Frontiers in microbiology · 2024Article
- Article
- The Role of Apoptin in Chicken Anemia Virus Replication.Pathogens (Basel, Switzerland) · 2020Review
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Authors and funding
8 authors.
Funding
Abstract
backgroundChicken anaemia virus (CAV) is commonly found in poultry. VP1 is the sole structural protein of CAV, which is the major component responsible for capsid assembly. The CAV virion consists of the VP1 protein and a viral genome. However, there is currently no information on the protein-nucleic acid interactions between VP1 and DNA molecules.
resultsIn this study, the recombinant VP1 protein of CAV was expressed and purified to characterize its DNA binding activity. When VP1 protein was incubated with a DNA molecule, the DNA molecule exhibited retarded migration on an agarose gel. Regardless of whether the sequence of the viral genome was involved in the DNA molecule, DNA retardation was not significantly influenced. This outcome indicated VP1 is a DNA binding protein with no sequence specificity. Various DNA molecules with different conformations, such as circular dsDNA, linear dsDNA, linear ssDNA and circular ssDNA, interacted with VP1 proteins according to the results of a DNA retardation assay. Further quantification of the amount of VP1 protein required for DNA binding, the circular ssDNA demonstrated a high affinity for the VP1 protein. The preferences arranged in the order of affinity for the VP1 protein with DNA are circular ssDNA, linear ssDNA, supercoiled circular dsDNA, open circular DNA and linear dsDNA.
conclusionsThe results of this study demonstrated that the interaction between VP1 and DNA molecules exhibited various binding preferences that were dependent on the structural conformation of DNA. Taken together, the results of this report are the first to demonstrate that VP1 has no sequence-specific DNA binding activity. The particular binding preferences of VP1 might play multiple roles in DNA replication or encapsidation during the viral life cycle.
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