There are several viruses that are not currently covered by efficient antiviral terapies, as towards Poliovirus and the new Covid19. The spread of atypical viral strains strongly raises the need of having efficient terapies with wide coverage against viruses.
In the following experiments it was used a composition comprising Glutathione Reductase (GSSG-r) and Oxidized Glutathione (GSSG), which we call GR compound, for pharmaceutical use as antiviral, in vitro, towards RNA nad DNA virus, and in vivo towards a Swine Flu Virus (H1N1) adapted to the mouse.

Glutathione is present in the cells in form of Reduced Glutathyione (GSH) and Oxidized Glutathyione (GSSG). The GSH:GSSG ratio indicates the antioxidant capacity of the cell and it is maintained in favour of GSH due to GSSG-r, an enzyme belonging to the class of oxidoreductase which rigenerates GSH starting from GSSG.

The GR compound binds to the membrane of cells infected with virus, and repolarizes the membranes so that the Glutamate comes back in the cell and the synthesis of Glutathione starts again. Maintaining a correct GSH:GSSG ratio is an essential requirement for the vitality and survival of the cell. This technology exerts its primary action electrochemically (oxidation-reductive state) both in the host cell and in the virus. Practically the virus, entering the cell, depolarises the cell membrane thus preventing the entry of Glutamate (due to the inhibition of its transport carrier), which is fundamental for the synthesis of Glutathione.

Glutathione continuosly passing from reduced to oxidized generates and maintains the reductive-oxide state, necessary for the cell; all this leads to the non-formation of the sulfur bridges of viral proteins, which thus, changed in allosterism and spatial configuration, are completely eliminated by the immune system; all viruses are weakened, HIV, Covid19, Polio, Ebola, because all viruses must go through this step: the protein formation.