Specific toxins destabilize virus inhibitors (e.g. AIDS viruses).
There are two approaches to the study of viral infections - the A-Z hypothesis of Sprietsma involving thiol-zinc inhibition of protease activation in the virus coat, and the activity of toxins in depleting the cell of thiols, or the activity of toxins activating (not detoxifying) the mixed function oxidase (MFO) system. Both of these systems generate free radicals and utilize thiols in the process. Zinc forms stable mercaptides with thiols, inhibits cyclic reduction-autoxidation of thiols and superoxide generation. When the MFO system acts as an activator and not as a detoxifier in that intermediate products are more toxic than the original compound, zinc inhibits the oxidation. An example of increased toxicity with increased MFO activity is the toxin 3-methylindole (3-MI), a toxic product of intestinal bacterial putrefaction which reactivates the infectious bovine rhinotracheitis virus (IBR). Zinc reduces MFO activity and in this regard it functions synergistically with antioxidants in protecting cell membranes. It is hypothesized that stable zinc complexes inhibit activity of proteases in the virus nucleocapside (NC) proteins in the virus coat, both directly and indirectly because zinc also inactivates some toxins that are thiol depleters or virus reactivators.
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D000818:Animals; D000998:Antiviral Agents / Q000037:antagonists & inhibitors* / Q000737:chemistry; D002417:Cattle; D003300:Copper / Q000502:physiology; D003545:Cysteine / Q000502:physiology; D005978:Glutathione / Q000502:physiology; D006678:HIV / Q000502:physiology*; D014118:Toxins, Biological / Q000494:pharmacology*; D015032:Zinc / Q000502:physiology
D000998:Antiviral Agents; D014118:Toxins, Biological; D003300:Copper; D005978:Glutathione; D015032:Zinc; D003545:Cysteine