Free chlorine reacts with viral proteins, but the protein structural determinants of viral resistance to chlorine treatment remain poorly understood. Here, we curated a dataset of 498 icosahedral virus structures, including intact virions and virus-like particles (VLPs), from the Protein Data Bank. Surprisingly, only 6.6% of these structures are associated with published viral chlorine inactivation rate constants (kobs). In these matched cases representing 12 virus families, total and maximum solvent accessible surface areas (SASA) of methionine residues within viral attachment and entry proteins were found to explain 78% of the variation in median kobs, suggesting a critical role of methionine exposure in viral resistance. For all the curated structures, fuzzy c-means clustering upon total and maximum SASA profiles of seven chlorine-reactive residues demonstrates that the common surrogate panel (MS2, PhiX174, Phi6, PRD1, and PR772) fails to represent the SASA diversity of human viruses. Instead, VLPs and novel non-tailed phages may serve as better surrogates for chlorine treatment due to SASA profile similarities to human viruses. Our findings highlight that the SASA features of residues provide a quantitative baseline for screening viral resistance to chlorine and offer a data-driven strategy to identify more structurally representative virus surrogates for future disinfection studies.
Zhu, C., Prinsen, K., Ward, L., Chaplin, M., Shen, M., Torii, S., Kauffman, K., Ye, Y.
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