Division of Plant Science and Technology, University of Missouri, Columbia, MO, 65211, USA.
Division of Plant Science and Technology, University of Missouri, Columbia, MO, 65211, USA.
Virology. 2024 Dec;600:110240. doi: 10.1016/j.virol.2024.110240. Epub 2024 Sep 11.
The P6 protein of cauliflower mosaic virus (CaMV) is a multifunctional protein that forms the electron dense, amorphous inclusion bodies that accumulate in the cytoplasm and has been shown to physically interact with all other CaMV proteins, including the CaMV movement protein (P1). In this study, we have investigated the subcellular localization of the P6 and P1 proteins in transient expression assays in Nicotiana benthamiana, as well as the influence of P6 on the expression and subcellular localization of P1. A version of P6 tagged with RFP was shown to envelop the endoplasmic reticulum (ER), whereas P1 tagged with RFP was shown to induce the fragmentation of the ER. Co-expression of P6 with P1 led to an enhancement of the spatial and temporal expression of P1, with a shift from expression through the plasma membrane and interior of the cell to punctate spots associated with the cell wall.
花椰菜花叶病毒（CaMV）的 P6 蛋白是一种多功能蛋白，它形成电子致密、无定形的包含体，在细胞质中积累，并已被证明与所有其他 CaMV 蛋白（包括 CaMV 运动蛋白（P1））发生物理相互作用。在这项研究中，我们研究了 P6 和 P1 蛋白在 transient expression assays 中在 Nicotiana benthamiana 中的亚细胞定位，以及 P6 对 P1 的表达和亚细胞定位的影响。标记有 RFP 的 P6 版本被证明包裹内质网（ER），而标记有 RFP 的 P1 则被证明诱导 ER 的碎片化。P6 与 P1 的共表达导致 P1 的时空表达增强，从通过质膜和细胞内部表达转变为与细胞壁相关的点状斑点。
