Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, Ciudad Politécnica de la Innovación, Ed. 8E. Camino de Vera s/n, 46022 Valencia, Spain.
Virology. 2011 May 10;413(2):310-9. doi: 10.1016/j.virol.2011.03.001. Epub 2011 Mar 27.
Two small viral proteins (DGBp1 and DGBp2) have been proposed to act in a concerted manner to aid intra- and intercellular trafficking of carmoviruses though the distribution of functions and mode of action of each protein partner are not yet clear. Here we have confirmed the requirement of the DGBps of Pelargonium flower break virus (PFBV), p7 and p12, for pathogen movement. Studies focused on p12 have shown that it associates to cellular membranes, which is in accordance to its hydrophobic profile and to that reported for several homologs. However, peculiarities that distinguish p12 from other DGBps2 have been found. Firstly, it contains a leucine zipper-like motif which is essential for virus infectivity in plants. Secondly, it has an unusually long and basic N-terminal region that confers RNA binding activity. The results suggest that PFBV p12 may differ mechanistically from related proteins and possible roles of PFBV DGBps are discussed.
两种小的病毒蛋白（DGBp1 和 DGBp2）被提议协同作用，以帮助 carmoviruses 在细胞内和细胞间的运输，尽管每个蛋白伴侣的功能分配和作用模式尚不清楚。在这里，我们已经证实 Pelargonium flower break virus (PFBV) 的 DGBps、p7 和 p12 对病原体运动的要求。对 p12 的研究表明，它与细胞膜结合，这与它的疏水性特征以及几个同源物的报道相符。然而，p12 与其他 DGBps2 区分开来的特殊性已经被发现。首先，它包含一个亮氨酸拉链样基序，这对于病毒在植物中的感染性是必不可少的。其次，它有一个异常长的碱性 N 端区域，赋予 RNA 结合活性。结果表明，PFBV p12 在机制上可能与相关蛋白不同，并讨论了 PFBV DGBps 的可能作用。
