Bombyx mori nucleopolyhedrovirus encodes a DNA-binding protein capable of destabilizing duplex DNA

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V S Mikhailov1, A L Mikhailova, M Iwanaga

  • 1N. K. Koltzov Institute of Developmental Biology, Moscow, Russia. vsmikha@postman.riken.go.jp

Journal of Virology
|April 3, 1998
PubMed

Insights

A novel DNA-binding protein (DBP) from Bombyx mori nucleopolyhedrovirus (BmNPV) was identified and characterized. This protein preferentially binds single-stranded DNA and can unwind DNA duplexes, suggesting a role in viral replication.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Bombyx mori nucleopolyhedrovirus (BmNPV) is a significant insect pathogen.
  • Understanding viral protein functions is crucial for insect pest control strategies.

Purpose of the Study:

  • To purify and characterize a novel DNA-binding protein (DBP) from BmNPV.
  • To elucidate the DNA-binding properties and potential function of BmNPV DBP.

Main Methods:

  • Protein purification from infected BmN cells.
  • Peptide sequencing and homology analysis to identify the gene encoding DBP.
  • In vitro DNA binding and DNA unwinding assays.

Main Results:

  • A 38 kDa DNA-binding protein (DBP) was purified from BmNPV-infected cells.
  • DBP is encoded by ORF16 (dbp) and is a homolog of AcMNPV ORF25.
  • DBP binds preferentially to single-stranded DNA, protects it from exonuclease digestion, and exhibits DNA helix-destabilizing activity.

Conclusions:

  • BmNPV DBP is a single-stranded DNA-binding protein with DNA unwinding capabilities.
  • DBP likely plays a role in viral DNA replication and/or other DNA metabolism processes during BmNPV infection.

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