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A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

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Published on: April 11, 2014

Phage-inactivating Effect of Iron(II)-Ascorbate Complex.

I H Lho^1,2, K Morita¹, H Miyake¹

¹a Department of Applied Biological Sciences , Saga University , Saga 840 , Japan.

Bioscience, Biotechnology, and Biochemistry

|June 11, 2016

Summary

The iron(II)-ascorbate complex effectively inactivates various phages by damaging their DNA. This inactivation mechanism involves oxygen radicals and DNA strand breakage.

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Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

Bacteriophages are viruses that infect bacteria.
Understanding phage inactivation mechanisms is crucial for phage therapy and diagnostics.

Purpose of the Study:

To investigate the inactivating effect of the iron(II)-ascorbate complex on various phages.
To elucidate the mechanism underlying phage inactivation by this complex.

Main Methods:

Testing the complex's efficacy against nine different phages.
Studying the inactivation mechanism of phage J1 using various chemical agents and conditions.
Analyzing the effect of the complex on DNA structure using techniques like SDS-PAGE and DNA electrophoresis.

Main Results:

The iron(II)-ascorbate complex inactivated all nine tested phages at 10^-6 M.
Inactivation was enhanced by H2O2 or Cu(2+) and prevented by nitrogen bubbling, Fe(3+), reducing agents, chelating agents, or radical scavengers, suggesting oxygen radical involvement.
The complex caused single- and double-stranded breaks in supercoiled and linear DNA from various sources (pUC18, M13mp8, λDNA, J1 DNA).
No alterations were observed in the SDS-PAGE pattern or amino acid composition of bovine serum albumin or phage J1 structural proteins.

Conclusions:

The iron(II)-ascorbate complex is a potent phage inactivating agent.
Oxygen radicals mediate the inactivation process.
DNA strand breakage is the primary mechanism responsible for phage inactivation by this complex.