Kiselyova Olga I, Yaminsky Igor V, Karpova Olga V, Rodionova Nina P, Kozlovsky Stanislav V, Arkhipenko Marina V, Atabekov Joseph G
Faculty of Physics, Faculty of Chemistry of Moscow State University, 119992 Moscow, Russia.
J Mol Biol. 2003 Sep 12;332(2):321-5. doi: 10.1016/s0022-2836(03)00835-0.
Recently we have reported that a selective binding of potato virus X (PVX)-coded movement protein (termed TGBp1 MP) to one end of a polar coat protein (CP) helix converted viral RNA into a translatable form and induced a linear destabilization of the whole helical particle. Here, the native PVX virions, RNase-treated (PVX(RNA-DEG)) helical particles lacking intact RNA and their complexes with TGBp1 (TGBp1-PVX and TGBp1-PVX(RNA-DEG)), were examined by atomic force microscopy (AFM). When complexes of the TGBp1 MP with PVX were examined by means of AFM in liquid, no structural reorganization of PVX particles was observed. By contrast, the products of TGBp1-dependent PVX degradation termed "beads-on-string" were formed under conditions of AFM in air. The AFM images of PVX(RNA-DEG) were indistinguishable from images of native PVX particles; however, the TGBp1-dependent disassembly of the CP-helix was triggered when the TGBp1-PVX(RNA-DEG) complexes were examined by AFM, regardless of the conditions used (in air or in liquid). Our data supported the idea that binding of TGBp1 to one end of the PVX CP-helix induced linear destabilization of the whole helical particle, which may lead to its disassembly under conditions of AFM.
最近我们报道，马铃薯X病毒（PVX）编码的运动蛋白（称为TGBp1 MP）与极性衣壳蛋白（CP）螺旋的一端选择性结合，可将病毒RNA转化为可翻译形式，并诱导整个螺旋粒子线性去稳定化。在此，通过原子力显微镜（AFM）对天然PVX病毒粒子、经核糖核酸酶处理的（PVX(RNA-DEG)）缺乏完整RNA的螺旋粒子及其与TGBp1的复合物（TGBp1-PVX和TGBp1-PVX(RNA-DEG)）进行了检测。当在液体中通过AFM检测TGBp1 MP与PVX的复合物时，未观察到PVX粒子的结构重组。相比之下，在空气中进行AFM检测的条件下形成了依赖TGBp1的PVX降解产物，称为“串珠状”。PVX(RNA-DEG)的AFM图像与天然PVX粒子的图像无法区分；然而，当通过AFM检测TGBp1-PVX(RNA-DEG)复合物时，无论使用何种条件（在空气中或在液体中），都会触发依赖TGBp1的CP螺旋解体。我们的数据支持这样一种观点，即TGBp1与PVX CP螺旋的一端结合会诱导整个螺旋粒子线性去稳定化，这可能导致其在AFM条件下解体。
