Dissident AIDS Database

Co-factorsStressOxidative stressHIV
 Foster Harold D.
  E. W. Taylor and his colleagues at the University of Georgia discovered in the mid-1990s there was a series of viruses that encoded for a selenium-dependent glutathione peroxidase. These included HIV-1 and HIV-2, Coxsackievirus B, and the hepatitis B and C viruses (Taylor, E.W. and others, "HIV-1 encodes a sequence overlapping env.gp41 with highly significant similarity to selenium dependent glutathione peroxidases", Journal of AIDS and Human Retrovirology 1997; 15(5):393-394, Taylor, E.W. and others, "Genomic structures of viral agents in relation to the biosynthesis of selenoproteins", Biological Trace Element Research 1997; 56(1):63-91, Taylor, E.W., "Selenium and viral diseases: facts and hypotheses", J. Orthomolecular Medicine 1997; 12(4):227-239). What this means is that the genomes of such viruses include a gene that is virtually identical to that seen in humans, which allows them to manufacture the essential enzyme glutathione peroxidase. Subsequently, to prove that this apparent section of the HIV-1 genetic code really permitted it to produce the mammalian selenoenzyme glutathione peroxidase, Taylor and his co-workers cloned the hypothetical HIV-1 gene and transfected canine kidney cells and MCF7 cells with it (Zhao, L. and others, "Molecular modeling and in vitro activity of an HIV-1- encoded glutathione peroxidase", Proc Natl Acad Sci USA 2000 June 6; 97(12):6356-6361). In both cases, the cells given the HIV-1 gene greatly increased their production of the selenoprotein glutathione peroxidase. This proves beyond any reasonable doubt that HIV-1 is capable of producing glutathione peroxidase for its own purposes. Recently in my book (Foster, H.D., What Really Causes AIDS, Trafford, Victoria BC, 2002), I put forward an alternative hypothesis that not only explains why HIV-1 takes so long to cause AIDS but why this disease has the specific symptoms it does. It was suggested that since HIV-1 encodes for the human selenoenzyme glutathione peroxidase, as it is replicated its genetic needs cause it to deprive seropositive individuals not only of glutathione peroxidase but also of its four basic components: selenium, cysteine, glutamine and tryptophan. Eventually, after a period of time (the length of which depends on the diet being eaten), this depletion process causes severe deficiencies of all these nutrients. In 1981, Bunk and Combs described an experiment demonstrating that, in chickens, selenium deficiency impaired the conversion of the S–amino acid methionine into cysteine (Bunk, M.J. and others, "Evidence for an impairment in conversion of methionine to cysteine in the Se-deficient chicken", Proc Soc Ex Biol Med 1981; 167:87-93). It is highly likely that this is true for humans. If it is, then, by encoding for the selenoenzyme glutathione peroxidase, HIV-1 causes a deficiency of cysteine in infected individuals in two distinct ways. Firstly, the virus removes cysteine directly from the body as it replicates. Secondly, it creates a selenium deficiency which impairs the conversion of methionine to cysteine, so reducing the availability of the latter. Simply put, HIV-1 both increases the demand for and reduces the supply of cysteine in patients who are HIV-1 positive.
  Nexus Magazine, Volume 11, Number 1 (December-January 2004)2004