Chlorine dioxide reactivity with proteins

Abstract

Studies were conducted to evaluate chlorine dioxide reactivity with proteins and the role of these reactions in the inactivation of the bacterial virus f2 with chlorine dioxide. The effect of chlorine dioxide on the ability of f2 to specifically attach to its host Escherichia coli K13 was compared to the inactivation of virus during the initial seconds of contact time. At pH 7.2 and and 5°C, the virus was rapidly inactivated with 0.6 mg l −1 of chlorine dioxide. Approximately 2 log units of inactivation were observed within 30 s. The loss of protein specific attachment function nearly paralleled intact virus inactivation with 1.2 log units of attachment inhibition occurring within 30 s. The inactivation of virus and the inhibition of specific attachment both increased with increasing pH and increasing disinfectant concentration. Inactivation of f2 was hypothesized to occur as the result of chlorine dioxide reacting with discrete chemical moieties in the viral protein. Cysteine, tyrosine and tryptophan reacted with chlorine dioxide within a time frame that could affect viral inactivation. In denatured f2 capsid protein monomers, these amino acids were almost totally degraded within 2 min by chlorine dioxide. Only tyrosine reacted with chlorine dioxide following treatment of the intact virion with disinfectant. Even though the degradation of tyrosine residues occurred at a much slower rate than the rate of virus inactivation, the protein component of f2 virus appeared to be the site of the lethal lesion produced by chlorine dioxide. These tyrosine reactions with chlorine dioxide appeared to alter the virus such that specific attachment was inhibited.