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Journal of Immunology Research
Volume 2017, Article ID 7407136, 16 pages
Research Article

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

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia
2Gamaleja Research Center of Epidemiology and Microbiology, Moscow, Russia
3Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden
4Chemistry Department, Belozersky Research Institute of Physico-Chemical Biology of Lomonosov Moscow State University, Moscow, Russia
5Linköping University, Linköping, Sweden
6Riga Stradins University, Riga, Latvia
7M.P. Chumakov Institute of Poliomyelitis and Viral Encephalities, Russian Academy of Sciences, Moscow, Russia

Correspondence should be addressed to Anastasia Latanova; moc.liamg@avonatalaa

Received 28 December 2016; Accepted 13 April 2017; Published 22 June 2017

Academic Editor: Masha Fridkis-Hareli

Copyright © 2017 Anastasia Latanova et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Figure S1. Enzymatic activity of reverse transcriptase of HIV‐1 strain HXB2 (WT) and its variant inactivated by D185N, D186N and E478Q mutations (Mutant) purified as p51/p66 heterodimers in vitro tests of polymerase (A) and RNAse H activity (B, C). Influence of concentration of RT and inactivated RT on their RNase H activity visualized by the analysis of the products of RNAse H activity by PAGE (B); quantitative analysis of the activities (C). Solid dots and lines refer to the wild type, and hollow dots and dash lines, to inactivated RT. Figures represent the results of three independent experiments.

  1. Supplementary material