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Subtle differences in virus composition affect disinfection kinetics and mechanisms - PubMed
Subtle differences in virus composition affect disinfection kinetics and mechanisms - PubMed
****!!!!*** "Chlorine Dioxide caused great variability in the inactivation kinetics between viruses and was the only treatment that did not induce genome damage... ClO2 rapidly degraded the capsid proteins of all three viruses. Protein composition alone could not explain the observed degradation trends; instead, molecular dynamics simulations indicated that degradation is dictated by the solvent-accessible surface area of individual amino acids. Finally, despite the similarities of the three viruses investigated, *****their mode of inactivation by a single disinfectant varied. This explains why closely related viruses can exhibit drastically different inactivation kinetics."
·pubmed.ncbi.nlm.nih.gov·
Subtle differences in virus composition affect disinfection kinetics and mechanisms - PubMed
Inactivation of influenza virus haemagglutinin by chlorine dioxide: oxidation of the conserved tryptophan 153 residue in the receptor-binding site | Microbiology Society
Inactivation of influenza virus haemagglutinin by chlorine dioxide: oxidation of the conserved tryptophan 153 residue in the receptor-binding site | Microbiology Society
2012. by Norio Ogata. Airborne influenza virus infection of mice can be prevented by gaseous chlorine dioxide (ClO2). This study demonstrated that ClO2 abolished the function of the haemagglutinin (HA) of influenza A virus (H1N1) in a concentration-, time- and temperature-dependent manner. The IC50 during a 2 min reaction with ClO2 at 25 °C was 13.7 µM, and the half-life time of HA with 100 µM ClO2 at 25 °C was 19.5 s. Peptides generated from a tryptic digest of ClO2-treated virus were analysed by mass spectrometry. An HA fragment, 150NLLWLTGK157 was identified in which the tryptophan residue (W153) was 32 mass ...
·microbiologyresearch.org·
Inactivation of influenza virus haemagglutinin by chlorine dioxide: oxidation of the conserved tryptophan 153 residue in the receptor-binding site | Microbiology Society