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Published on: November 1, 2011
[Analysis and expression of Hyphantria cunea nuclear polyhedrosis virus sod gene]
Abstract:
The sequencing results indicated that Hyphantria cunea nuclear polyhedrosis virus (HcNPV) sod gene open reading frame of 456 nt encoding protein of 151 amino acid, was identified to that of Bombyx mori nuclear polyhedrosis virus (BmNPV), and exhibited 97.2% homology at nucletde level to that of Autographa californica nuclear polyhedrosis virus (AcNPV), three amino acid residues difference in amino acid level with AcNPV sod. The essential amino acid residues for the construction and active could be detected in HcNPV sod. Activity of the SOD is 147.09 U per milliliter E. coli.
Insights
Hyphantria cunea nuclear polyhedrosis virus (HcNPV) sod gene sequencing revealed high homology to related viruses. The HcNPV superoxide dismutase (SOD) enzyme is essential and active, showing potential for biotechnological applications.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Nuclear polyhedrosis viruses (NPVs) are significant insect pathogens.
- The superoxide dismutase (SOD) enzyme plays a crucial role in oxidative stress defense.
- Understanding viral gene functions is key to developing biopesticides.
Purpose of the Study:
- To sequence and characterize the sod gene of Hyphantria cunea nuclear polyhedrosis virus (HcNPV).
- To compare the HcNPV sod gene and its encoded protein with those from other NPVs.
- To assess the functional activity of the HcNPV-encoded SOD enzyme.
Main Methods:
- DNA sequencing of the HcNPV sod gene open reading frame (ORF).
- Homology analysis at nucleotide and amino acid levels with Bombyx mori NPV (BmNPV) and Autographa californica NPV (AcNPV).
- Expression of HcNPV sod in E. coli and measurement of SOD activity.
Main Results:
- The HcNPV sod gene ORF is 456 nt, encoding a 151 amino acid protein.
- High nucleotide homology (97.2%) was observed between HcNPV sod and AcNPV sod.
- Essential amino acid residues for SOD function were identified in HcNPV sod, with activity measured at 147.09 U/mL in E. coli.
Conclusions:
- The HcNPV sod gene is highly conserved among NPVs, particularly with AcNPV.
- The HcNPV-encoded SOD enzyme possesses essential functional residues and significant enzymatic activity.
- These findings support the potential use of HcNPV sod in molecular biology and biotechnology.
