In this study bNab were induced, although the potency of the responses was generally low. The soluble gp140 used in those studies comprised R2 gp120 fused in sequence to the gp41 ectodomain as a result of mutation of the furin protease site that normally at which gp160 is normally cleaved into its subunits. The gp140 was produced in non-human primate cell culture infected with recombinant vaccinia virus expressing the modified Env gene. Although the gp140 released by lysis of the infected cells was extensively purified, the immunogen was still contaminated with cellular proteins that induced antibodies reactive with human cell proteins Alphalipoic-acid present on viruses tested in neutralization assays. The gp140 produced using this method was predominantly dimeric, with some trimer and less monomer. Both hBD-4 mutants are predicted to have no functional peptide because of changes in the protein sequence. No structure prediction could be performed for this mutant because its structure is not available. One form was of the same sequence as that used previously, and was purified so that the monomeric, dimeric, and Isoniazid trimeric forms were retained in the immunogen, as previously.Our objective was to investigate if along the process of putatively the levels of these key molecules increase, decrease or remain stable.For this purpose, we examined individuals without clinical evidence of neurological disease or significant neurodegenerative disease changes and differentiated solely according to age: young adult, middleaged and oldest-old.