#$%^&*AU2017101237A420180531.pdf#####The high affinity mutant HIV- 1 envelope glycoprotein mu gp120 can function as a vaccine and a curative against HIV- 1 Norbert 0. Temajo, Ph.D. Abstract The longing of mankind is currently for the world of Scientists to invent a cheap successful vaccine against the human immunodeficiency virus type 1 (HIV-1). Workers in this field, adorned with the memory of the eradication of the pox virus and now nearly also of the poliovirus, had anticipated that they could easily replicate the techniques based on the neutralization antibodies against the HIV-1. Alas: the calculated neutralization antibodies foray has not been to be, and to date there are no such vaccines! It so happens, however, that the immunodeficiency virus attacks the host's CD4+ T-cells in a protein-protein interaction event whereby the HIV-1 envelope glycoprotein gp120 recognizes and strikes residence on the CD4 receptor and CCR5/CXCR4 co-receptors sites on the CD4+ T-cells, followed by the viral multiplication and destruction of these cells. This protein-protein interaction has been exploited and experts have designed small chemical molecules as drugs to interfere with or inhibit the interactions. But the inherent disadvantages are that these drugs are very expensive (in fact too expensive) for dwellers in the developing Countries, and furthermore the drugs exhibit undesirable clinical side effects. On our part, we were enticed to conjure the notion that if we could create a gp120 mutant (mu gp120) with an excessively high affinity for the CD4 receptor and CCR5/CXCR4 co-receptors sites on CD4+ T-cells then the mutant gp120 released into the blood stream of a host following vaccination of the host with it would out-compete the HIV-1 for, and sterically hinder, the receptor and co-receptors sites on the CD4+ T-cells, thus saving the T-cells from being infected (transduced) and destroyed by the viral multiplication. The mutant gp
