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Abstract
ABSTRACTPlant viruses cross the barrier of the plant cell wall by moving through intercellular channels, termed plasmodesmata, to invade their hosts. They accomplish this by encoding movement proteins (MPs), which act to alter plasmodesmal gating. How MPs target to plasmodesmata is not well understood. Our recent characterization of the first plasmodesmal localization signal (PLS) identified in a viral MP, namely, the MP encoded by the Tobamovirus Tobacco mosaic virus (TMV), now provides the opportunity to identify host proteins that recognize this PLS and may be important for its plasmodesmal targeting. One such candidate protein is Arabidopsis synaptotagmin A (SYTA), which is required to form endoplasmic reticulum (ER)-plasma membrane contact sites and regulates the MP-mediated trafficking of begomoviruses, tobamoviruses, and potyviruses. In particular, SYTA interacts with, and regulates the cell-to-cell transport of, both TMV MP and the MP encoded by the Tobamovirus Turnip vein clearing virus (TVCV). Using in planta bimolecular fluorescence complementation (BiFC) and yeast two-hybrid assays, we show here that the TMV PLS interacted with SYTA. This PLS sequence was both necessary and sufficient for interaction with SYTA, and the plasmodesmal targeting activity of the TMV PLS was substantially reduced in an Arabidopsis syta knockdown line. Our findings show that SYTA is one host factor that can recognize the TMV PLS and suggest that this interaction may stabilize the association of TMV MP with plasmodesmata.
Highlights
Plant viruses cross the barrier of the plant cell wall by moving through intercellular channels, termed plasmodesmata, to invade their hosts
We expected that a plasmodesmal localization signal (PLS)-interacting protein involved in Pd targeting would possess at least two important features: it would be located in close proximity to the plasma membrane, in which Pd are known to reside [16], and it would be known to interact with full-length Tobacco mosaic virus (TMV) movement proteins (MPs) and be required for MP intercellular movement
We examined whether synaptotagmin A (SYTA) interacted with TMV MP1–50 and whether this interaction was impaired in either of the two known single-amino-acid-substitution mutants in the PLS that do not target to Pd, MP1–50(V4A) and MP1–50(F14A) [13]
Summary
Plant viruses cross the barrier of the plant cell wall by moving through intercellular channels, termed plasmodesmata, to invade their hosts. Our recent characterization of the first plasmodesmal localization signal (PLS) identified in a viral MP, namely, the MP encoded by the Tobamovirus Tobacco mosaic virus (TMV), provides the opportunity to identify host proteins that recognize this PLS and may be important for its plasmodesmal targeting One such candidate protein is Arabidopsis synaptotagmin A (SYTA), which is required to form endoplasmic reticulum (ER)-plasma membrane contact sites and regulates the MP-mediated trafficking of begomoviruses, tobamoviruses, and potyviruses. We recently identified the first plasmodesmal localization signal (PLS) in a viral MP, located within the N-terminal 50 amino acid residues of the TMV MP (MP1–50) [13] This allows us to identify host cell proteins that recognize MP1–50 and which may facilitate TMV MP targeting to or association with Pd. This allows us to identify host cell proteins that recognize MP1–50 and which may facilitate TMV MP targeting to or association with Pd One such candidate protein is Arabidopsis synaptotagmin A (SYTA), which is required to form endoplasmic reticulum-plasma membrane (ER-PM) contact sites in Arabidopsis thaliana [14]. SYTA appears to be a host cell factor that can recognize the PLS in TMV MP1–50 and stabilize MP association with Pd
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