Fusion to Flaviviral Leader Peptide Targets HIV-1 Reverse Transcriptase for Secretion and Reduces Its Enzymatic Activity and Ability to Induce Oxidative Stress but Has No Major Effects on Its Immunogenic Performance in DNA-Immunized Mice

<div>Schematic representation of chimeric drug-resistant HIV-1 reverse transcriptase carrying the N-terminal insertion of the N-terminal signal peptide of NS1 protein of TBEV (RT1.14oil). Rectangular boxes stand for polypeptide chains of NS1 with leader signal peptide (white) and RT1.14opt-in sequence (gray) with amino acid substitutions in polymerase (D185N, D186N) and RNase H signature motives (E478Q) leading to inactivation of respective enzymatic activities in the resultant RT1.14oil polyprotein. Amino acid positions in the polypeptide chain are designated with numbers.</div>

Journal of Immunology Research

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Figure 1

Figure 1: Fusion to Flaviviral Leader Peptide Targets HIV-1 Reverse Transcriptase for Secretion and Reduces Its Enzymatic Activity and Ability to Induce Oxidative Stress but Has No Major Effects on Its Immunogenic Performance in DNA-Immunized Mice 

Figure 1 | Fusion to Flaviviral Leader Peptide Targets HIV-1 Reverse Transcriptase for Secretion and Reduces Its Enzymatic Activity and Ability to Induce Oxidative Stress but Has No Major Effects on Its Immunogenic Performance in DNA-Immunized Mice 