Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide

Abstract

BackgroundCell mediated immunity, including efficient CTL response, is required to prevent HIV-1 from cell-to-cell transmission. In previous investigations, we have shown that B1 peptide derived by Fourier transformation of HIV-1 primary structures and sharing no sequence homology with the parent proteins was able to generate antiserum which recognizes envelope and Tat proteins. Here we have investigated cellular immune response towards a novel non-homologous peptide, referred to as cA1 peptide.Methodology/Principal FindingsThe 20 amino acid sequence of cA1 peptide was predicted using the notion of peptide hydropathic properties; the peptide is encoded by the complementary anti-sense DNA strand to the sense strand of previously described non-homologous A1 peptide. In this report we demonstrate that the cA1 peptide can be a target for major histocompatibility complex (MHC) class I-restricted cytotoxic T lymphocytes in HIV-1-infected or envelope-immunized individuals. The cA1 peptide is recognized in association with different MHC class I allotypes and could prime in vitro CTLs, derived from gp160-immunized individuals capable to recognize virus variants.Conclusions/SignificanceFor the first time a theoretically designed immunogen involved in broad-based cell-immune memory activation is described. Our findings may thus contribute to the advance in vaccine research by describing a novel strategy to develop a synthetic AIDS vaccine.

RRM Prediction of Erythrocyte Band3 Protein as Alternative Receptor for SARS-CoV-2 Virus

“…Once the characteristic biological function of the protein's functional group has been identified, it is possible to design new proteins with the desired frequency components and, consequently, with the desired biological functions [3][4][5][6]11,12]. This approach has already been successfully applied and experimentally tested in design of the FGF analogue [3][4][5]13], HIV envelope protein analogue [3][4][5][14][15][16] and a peptide to mimic the oncolytic function of the myxoma virus [17,18].…”

Analysis of Protein–Receptor Interactions on an Example of Leptin–Leptin Receptor Interaction Using the Resonant Recognition Model

“…The following protein sequences from the UniProt database have been analyzed using the RRM: Once the characteristic frequency for biological function of the protein is identified, it is possible to design de novo proteins with desired frequency components and subsequently with desired biological functions [1][2][3]6]. The design of bioactive peptides using the RRM concept has been already successfully experimentally tested in the design of FGF analogue [1][2][3][4], HIV envelope protein analogue [1][2][3][22][23][24], IL-12 analogue [25], and peptide to mimic Myxoma virus oncolytic function [26,27].…”

Specificity, polyspecificity, and heterospecificity of antibody‐antigen recognition

“…The specificity of interactions between two peptides is enhanced by the ability of amino acids to form complementary protrusions and cavities and by the presence of amino acids of opposite charge . In a recent application of the phenomenon of hydropathic complementarity to the study of human immunodeficiency virus type 1 (HIV‐1) immune responses, a complementary HIV gp120 antisense peptide of inverted hydropathy corresponding to the cA1 T cell epitope peptide was used to induce cellular immunity against HIV‐1 …”