Figures
There are errors in the Western blot panels of Fig. 4D and Fig. 5C. Please view the correct figures below.
(A) Schematic representation of the GagPol and GagPR constructs and their amino acid sequences of the p6* and p6 domains. The p6* domain was replaced by the p1+p6 domain (lacking the 12 C-terminal amino acids), and the resultant constructs were referred to as Gag(p6)Pol and Gag(p6)PR. The GagPol-HA and Gag(p6*)PR-HA constructs contain the authentic p6* domain (upper), and the Gag(p6)Pol and Gag(p6)PR constructs contain the p6 domain instead of the p6* (lower). All constructs contained inactive PR and were expressed in the context of pNL43. (B-E) HeLa cells were transfected with Gag(p6)Pol, Gag(p6)PR, GagPol-HA, and Gag(p6*)PR-HA constructs. (B) Membrane affinity of the Gag(p6)Pol and Gag(p6)PR proteins. Cells were subjected to membrane flotation centrifugation followed by Western blotting using anti-p24 antibody. (C) Intracellular localization of the Gag(p6)Pol and Gag(p6)PR proteins. Cells were immunostained with anti-p24 antibody (green), and nuclei were stained with TO-PRO-3 (blue). All micrographs are shown at the same magnification. In each sample, approximately 100 antigen-positive cells (from 3 independent experiments) were subjected to distribution pattern analysis. (D) Intracellular expression and viral particle production of the Gag(p6)Pol and Gag(p6)PR proteins. The Gag-FLAG/Pol-HA construct was used as a positive control. Cells and purified viral particles were subjected to Western blotting using anti-p24 antibody. Arrows indicate GagPol and GagPR. (E) Electron microscopy of cells transfected with Gag(p6*)PR-HA and Gag(p6)PR. The cells were stained with uranyl acetate and lead citrate. Arrowheads show pedestal-like structures. Bars, 500 nm.
(A) Schematic representation of GagPol-HA and its derivatives containing the Fyn(10) N-terminal sequence and the p6 domain. The initiation codon of GagPol-HA was replaced by Fyn(10) [referred to as Fyn(10)GagPol-HA] and the p6* domain was further replaced by the p6 domain [referred to as Fyn(10)Gag(p6)Pol-HA]. All constructs contained inactive PR. The letter m indicates a myristoylation site, and palm indicates a palmitoylation site. (B and C) HeLa cells were transfected with GagPol-HA, Fyn(10)GagPol-HA, and Fyn(10)Gag(p6)Pol-HA. (B) Intracellular localization of GagPol-HA derivatives. Cells were immunostained with anti-HA antibody (green or red) and nuclei were stained with TO-PRO-3 (blue). All micrographs are shown at the same magnification. (C) Intracellular expression and viral particle production. The Gag-FLAG/Pol-HA construct was used as a positive control. Cells and purified viral particles were subjected to Western blotting using anti-HA antibody.
Reference
Citation: The PLOS ONE Staff (2015) Correction: A Large Extension to HIV-1 Gag, Like Pol, Has Negative Impacts on Virion Assembly. PLoS ONE 10(1): e0117765. https://doi.org/10.1371/journal.pone.0117765
Published: January 21, 2015
Copyright: © 2015 The PLOS ONE Staff. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited