The impact of chlorine and heat on the infectivity and physicochemical properties of bacteriophage MS2. Issue 8 (5th June 2018)

• Record Type: Journal Article
• Authors: Brié, Adrien; Gantzer, Christophe; Boudaud, Nicolas; Bertrand, Isabelle
• Is Part Of: FEMS microbiology ecology. Volume 94:Issue 8(2018:Aug.)
• Publication Date: 2018-06-05
• Subjects: free chlorine -- heat -- MS2 bacteriophage -- surface properties -- hydrophobicity -- charge; Microbial ecology -- Periodicals; Microbiology -- Periodicals; 579.17
• DOI: 10.1093/femsec/fiy106
• Languages: English
• ISSNs: 0168-6496

Abstract

Abstract: Enteric viruses and bacteriophages are exposed to various inactivating factors outside their host, and among them chlorine and heat are the most commonly used sanitizer in water industry and treatment in the food industry, respectively. Using MS2 phages as models for enteric viruses, we investigated the impact of free chlorine and heat on their physicochemical properties. Free chlorine was first evaluated alone. No increase in either capsid permeability or hydrophobicity was observed. The negative surface charge slightly increased suggesting molecular changes in the capsid. However, a weakening of the capsid by chlorine was suggested by differential scanning fluorimetry. This phenomenon was confirmed when chlorination was followed by a heat treatment. Indeed, an increase in the inactivation of MS2 phages and the permeability of their capsids to RNases was observed. More interestingly, an increase in the expression of hydrophobic domains at the phage surface was observed, but only for phages remaining infectious. The chlorine-caused weakening of the capsid suggested that, for an optimal use, the oxidant should be followed by heat. The increased permeability to RNases and the expression of hydrophobic domains may contribute to the development or improvement of molecular methods specific for infectious enteric viruses. Abstract : Exposure of MS2 phage to free chlorine followed by heat leads to higher inactivation, permeability to RNases and availability of hydrophobic domains within the capsid than does chlorine applied alone.