To date, the mechanisms of virus inactivation by microbicides are not well understood. Several modes of inactivation have been studied quite superficially. High temperature treatment is known to induce major changes in quaternary protein structures, resulting in a loss of continuity of the viral capsid icosahedral geometry. Hypochlorite is considered an oxidizing and cross-linking agent that causes viral protein disintegration. Ultraviolet (UV), supposedly, targets a small portion of a protein molecule containing vulnerable amino acids with high photochemical lability to UV.  On the molecular level, the mechanism of inactivation was first studied with representatives of the genus Enterovirus. It was shown that structural differences in the VP1 region of these viruses are crucial for inactivation with glutaraldehyde. Sensitive and moderately sensitive enteroviruses exhibited lysine residues in the outermost DE and BC loops of VP1 major capsid protein, while resistant viruses had no lysine residues in the N-terminus, β-strand D, BC, DE, and G2H loops of VP1. The identity in the VP1 region of MNV and human NoV is less than 50% which suggests the possibility of substantial discrepancies in their sensitivity to inactivation. The discrepancies observed among seven genetically closely related enteroviruses raises concern that testing results obtained using surrogate pathogens, even closely related, may not always be adequately extrapolative to human viruses.

Volha  Dzyakanava, Ph.D., Manager of the Virology Laboratory

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