4.8 Article

Selected Mechanistic Aspects of Viral Inactivation by Peracetic Acid

Journal

ENVIRONMENTAL SCIENCE & TECHNOLOGY
Volume 55, Issue 23, Pages 16120-16129

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.est.1c04302

Keywords

peracetic acid; amino acid; virus capsid; virus inactivation; disinfection

Funding

  1. Osprey Foundation of Maryland
  2. NIH/NIH GI Core Center, Hopkins Digestive Diseases Basic & Translational Research Core Center [P30DK089502]

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The study found that PAA effectively inactivates viruses by targeting susceptible amino acids on capsid proteins, while having little impact on viral genomes. Viruses with higher total number of target amino acids in their capsid structures may be more susceptible to PAA reactions.
Peracetic acid (PAA) is an alternative to traditional wastewater disinfection as it has a high oxidation potential without producing chlorinated disinfection byproducts. Reports have shown the effectiveness of PAA to reduce waterborne viruses, but the mechanism of inactivation is understudied. This study evaluated PAA consumption by amino acids and nucleotides that are the building blocks of both viral capsids and genomes. Cysteine (>1.7 min(-1)) and methionine (>1.2 min(-1)) rapidly consumed PAA, while cystine (1.9 x 10(-2) min(-1)) and tryptophan (1.4 x 10(-4) min(-1)) reactions occurred at a slower rate. All other amino acids and nucleotides did not react significantly (p < 0.05) with PAA during experiments. Also, PAA treatment did not result in significant (p < 0.05) reductions of purified RNA from MS2 bacteriophage and murine norovirus. Data in this study suggest that PAA effectively inactivates viruses by targeting susceptible amino acids on capsid proteins and does not readily damage viral genomes. Knowledge of virus capsid structures and protein compositions can be used to qualitatively predict the relative resistance or susceptibility of virus types to PAA. Capsid structures containing a higher total number of target amino acids may be more susceptible to PAA reactions that damage structural integrity resulting in inactivation.

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