Intracellular Transport of Plant Viruses: Finding the Door out of the Cell  Schoelz James E. , Harries Phillip A. , Nelson Richard S.   Molecular Plant  Volume 4, Issue 5, Pages 813-831 (September 2011) DOI: 10.1093/mp/ssr070 Copyright © 2011 The Authors. All rights reserved. Terms and Conditions

Figure 1 Cellular Membranes and Virus Intra/Intercellular Movement. (A, B) Schematics of the host cell endomembrane system illustrate the association of virus proteins with a known movement function (black text) from both non-tubule-forming viruses (A) and tubule-forming viruses (B) with host membranes. Only those proteins whose localization has been demonstrated in plants are shown. Host proteins that are known to mediate such interactions are shown where applicable (green text). PVX and BSMV are shown as representatives of the potex-like and hordei-like viruses, respectively. There are additional virus proteins in these categories that associate with membranes but that are not included due to space limitations. DNAJ, class of chaperone proteins; Ara7, Rab5 GTPase ortholog and a marker for early endosomes; Syn, synaptotagmin, a clathrin-associated, SNARE-interacting protein; CRT, calreticulin; REM, remorin, a plasma membrane protein; KNOLLE, T-SNARE; PDLPs, plasmodesmal localized proteins; At-4/1, Arabidopsis protein localized to plasmodesmata. (C, D) The results of inhibiting secretory pathways with brefeldin A (BFA) treatments or dominant negative mutations (ex. Sar1, Arf1) on the movement of non-tubule-forming (C) and tubule-forming (D) viruses from the ER to the cell periphery. A blue arrow blocked with a red X denotes that these viruses do not move through the endomembrane secretory system, since BFA treatment and/or mutations did not inhibit the movement of these virus proteins to the cell periphery. An unblocked arrow indicates that these virus proteins do move through the secretory system, since BFA treatment and/or mutations did diminish movement. V, vacuole; G, Golgi apparatus; N, nucleus; ER, endoplasmic reticulum; C, chloroplast; Pex, peroxisome; EE, early endosome; LE, late endosome. * TOM1 associates with vacuolar and probably ER as well as other unidentified membranes. These membrane interactions may be mediated by the host membrane-associated protein TOM2A. Molecular Plant 2011 4, 813-831DOI: (10.1093/mp/ssr070) Copyright © 2011 The Authors. All rights reserved. Terms and Conditions