Mechanism of chlorine inactivation of DNA-containing parvovirus H-1.
An investigation was undertaken to determine the effect of chlorine on a small DNA-containing enteric virus. Parvovirus H-1 was exposed to sodium hypochlorite in a phosphate-buffered saline solution at pH 7. Then, the whole virion, the protein capsid, or the nucleic acid was subjected to analysis. The sedimentation rate of the chlorine-treated whole virus decreased from 110S to 43S. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the virus demonstrated the formation of higher-molecular-weight aggregates resulting from covalent cross-linking of the capsid proteins. Electron microscopic examination revealed that the DNA was extruded as a taillike structure which remained attached to the virus particle. Furthermore, the DNA was intact and still capable of in vitro replication. The adsorption of the chlorine-treated virions to host cells was inhibited, presumably due to the effect of chlorine on the particular spatial arrangement of the capsid proteins required for adsorption. Specific sites on these proteins had become highly reactive, indicating that the initial action of chlorine on parvovirus H-1 was on the viral capsid.
D002213:Capsid / Q000378:metabolism; D002713:Chlorine / Q000494:pharmacology*; D004279:DNA, Viral / Q000378:metabolism; D008854:Microscopy, Electron; D010321:Parvoviridae / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D014871:Water Microbiology; D014881:Water Supply
D004279:DNA, Viral; D002713:Chlorine