Related Experiment Videos
[Virion polypeptides of the nuclear polyhedrosis virus of the silkworm]
Abstract:
The nuclear polyhedrosis virus of the silkworm B. mori was obtained by dissolution of polyhedra at pH 10,5. It was shown that the virus particles contain a protease, which cleaves a few virion polypeptides during the dissolution of polyhedra under alkaline conditions. The proteolytic activity is inactivated by polyhedra treatment with phenylmethylsulfonylfluoride, diisopropylfluorophosphate, HgCl2 and at 80 degrees. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed 18 virion polypeptides with molecular weights ranging between 10000-110000. It was assumed that the virion includes the polyhedral protein and its fragments. A possible role of the polyhedral protein and its fragments in the virion is discussed.
Insights
Silkworm nuclear polyhedrosis virus contains a protease that degrades viral proteins during polyhedron dissolution. This protease activity is inhibited by specific chemicals and heat, suggesting its role in virus structure.
Area of Science:
- Virology
- Insect Pathology
- Molecular Biology
Context:
- Nuclear polyhedrosis virus (NPV) is a significant pathogen of the silkworm, Bombyx mori.
- Understanding NPV virion composition and assembly is crucial for developing effective biocontrol strategies.
- Polyhedra dissolution under alkaline conditions is a key step in viral infection.
Purpose:
- To investigate the presence and activity of a protease within B. mori NPV virions.
- To characterize the effect of this protease on virion polypeptides during polyhedron dissolution.
- To elucidate the potential role of the protease and polyhedral protein fragments in the virion.
Summary:
- B. mori NPV was isolated by dissolving polyhedra at pH 10.5.
- A virion-associated protease was identified, cleaving viral polypeptides during alkaline dissolution.
- Proteolytic activity was inhibited by phenylmethylsulfonylfluoride, diisopropylfluorophosphate, HgCl2, and heat (80°C).
- SDS-PAGE revealed 18 polypeptides (10-110 kDa), suggesting the virion contains polyhedral protein and fragments.
Impact:
- Provides insights into the molecular mechanisms of NPV infection and virion structure.
- Identifies a viral protease that may play a role in post-entry events.
- Contributes to the fundamental knowledge of baculovirus biology and pathogenesis.