Assessment of the Binding Characteristics of Human Immunodeficiency Virus Type 1 Glycoprotein120 and Host Cluster of Differentiation4 Using Digital Signal Processing

Abstract

Protein residues which contribute to bio-recognition and binding interaction between HIV Surface protein also called Glycoprotein120 (gp120) and Cluster of Differentiation4 (CD4) have been identified. However, this was with limited number of isolates. Notwithstanding, the particular HIV isolate that harbors the gp120 with the greatest binding force to the CD4 has not been investigated. In this paper, protein sequences of gp120 from 43 HIV-1 isolates, 5 isolates each from the HIV-2 and SIV as well as the CD4 of 25 HIV host organisms were analyzed using Resonant Recognition Method (RMM). The results re-confirmed that protein sequences of the HIV and CD4 share common spectral features in relation to bio-recognition and binding. From the large dataset of the HIV and SIV isolates used, MFA group M subtype B (HIV-1) isolate was found to have the greatest affinity for the CD4. Furthermore, the CD4 of the human and chimpanzee were established to possess about same level of binding force to the HIV gp120. Also the CD4 of other species offered more attractive force to another protein in such a manner that the approach taken in this study has also shown to be a useful and reliable tool for clear categorization of species. Finally, clinically experimented results were found to correlate with the computationally obtained results as the gp120 of the HIV-2 and SIV which were recognized to circumvent the CD4 during infection were found to have low peak amplitude. This low peak amplitude observed in the HIV-2 and SIV implies that they have weak affinity or attraction for the host CD4.