Inactivation Of Enteroviruses Research Articles

Inactivation of Enterovirus by Glutaraldehyde

A study on the rate of inactivation by glutaraldehyde of coxsackievirus was conducted using different concentrations, temperatures, and pH values. It was found, that 2 percent glutaraldehyde at pH 7.4 and 25 C, as recommended for a sporicide, reduced the titer of infectious virus by 2 log10U in 1 min or less. The reduction was not negatively affected by high concentrations of organic matter (serum and animal spillings) in the reaction mixtures.

Proteolytic and microbial inactivation of enteroviruses

Some enteroviruses are susceptible to proteolytic enzymes. Coxsackie virus type A-9 seems to be an extreme example of this. It was inactivated by proteolytic bacteria (notably Pseudomonas aeruginosa) in a limited survey. This inactivation could be distinguished from adsorption or aggregation of the virus particles: 14C label from the virus coat protein, but not 32P from the viral nucleic acid, was taken up by the bacterial cells.

Enzymes Produced by a Pseudomonas Species Which Inactivate Inhibitors of Certain Viral Hemagglutinins

Abstract Elastase and phospholipase C which were purified from cultures of a psychrophylic Pseudomonas sp. were examined for ability to inactivate certain viral hemagglutinin inhibitors present in human sera. Both enzymes were required for inactivation of enterovirus and reovirus inhibitors, but adenovirus inhibitors were inactivated by the elastase alone. The Pseudomonas sp. elastase had much greater inhibitor-destroying activity than did pancreatic elastase or Flavobacterium elastase; the activity of the Pseudomonas sp. phospholipase C was comparable to that of phospholipase C from Clostridium perfringens. Cohn fraction III-0 (containing predominantly β lipoprotein) and fraction IV-1 (containing predominantly α lipoprotein) both inhibited enterovirus hemagglutinins. Immunoelectrophoretic studies showed that the combination of Pseudomonas elastase and phospholipase C produced marked alterations in both the α1 and β lipoproteins in human sera. Kaolin absorption also removed both α1 and β lipoproteins. Both of these treatments inactivate enterovirus HA inhibitors. Treatment of sera with heparin-MnCl2 or dextran sulfate-CaCl2, which precipitate β lipoproteins, removed only a portion of the inhibitory activity for enterovirus hemagglutinins. These findings suggest that enterovirus hemagglutinin inhibitors are present in both α and β lipoproteins of human sera.

STABILITY OF VIRUSES IN LOW MOISTURE FOODS

Reovirus type 1, influenza virus type A, and parainfluenza virus type 3 persisted for ≤ 3 days in the low-moisture foods tested. Then enteroviruses tested persisted > 2 weeks at room temperature and > 2 months in the refrigerator. Where storage temperature was not constant, time-temperature effects were roughly cumulative. Inactivation of enteroviruses proceeded at an intermediate rate in foods stored at an intermediate temperature of 12 C. Polioviruses from feces and from tissue cultures were inactivated at comparable rates in foods. The inactivation rate of another enterovirus (ECHO-6) was similar. Neither the presence of feces nor of the fecal microflora seemed to influence the persistence of food-borne poliovirus. The moisture level in a food did not effect poliovirus inactivation under conditions of these tests. At reduced temperatures, virus was extremely stable in foods at pH ≥ 7. At pH 5.5, there was a complex interaction of protein and salt content upon virus stability. Poliovirus was inactivated 10−2 during freeze-drying of cream-style com. The remaining virus was quite stable during storage of the product at 5 C.

PHOTODYNAMIC INACTIVATION OF ENTEROVIRUSES.

Wallis, Craig (Baylor University College of Medicine, Houston, Tex.), and Joseph L. Melnick. Photodynamic inactivation of enteroviruses. J. Bacteriol. 89:41-46. 1965.-Enteroviruses are usually resistant to photodynamic inactivation, but they can be rendered completely photosensitive to proflavine at pH 9 to 10, if they are first purified by filtration through an anion resin. In addition, if enteroviruses are grown in cells maintained in a salt-glucose medium, they can be photosensitized. Of 38 enteroviruses tested, 10 were rendered completely photosensitive to proflavine, or toluidine blue, or both, and the remaining 28 viruses were sensitized, but to a lesser degree. The binding of dye to the virus can be reversed by lowering the pH.

Inactivation of enteroviruses by 2,3-dimercaptopropanol (BAL)

The infectivity of poliovirus types 1, 2, and 3 and the hemagglutinating activity of ECHO 7 virus were inactivated by 2,3-dimercaptopropanol (BAL). The infectivity of ECHO 7 virus was slightly reduced. An oxidized form of BAL was found to be responsible for virus inactivation. Inactivation of virus was reversed by treatment with mercaptoethanol, CN −, and alkaline pH. BAL interfered with adsorption of poliovirus to HeLa cell monolayers. The results suggest that an oxidized form of BAL inactivates the above enteroviruses by reacting with —SH groups of the virus protein and that disulfide bonds may be formed between virus and the inactivating compound.