STRUCTURAL ANALYSIS OF THE COAT AND GENOMIC RNA OF THE BACTERIAL VIRUS MS2

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 病毒的一个几乎普遍的特性是要求病毒外壳从惰性刚性保护性外层转变为能够在感染期间传递核酸的活化动态颗粒。 这一动态过程需要病毒外壳发生构象变化（Poranen、Daugelavicius 和 Bamford，2002）（Dryden 等，1993；Endrich、Gehrig 和 Gehrig，1999；Fuller 和 Lee，1992；Kirnbauer 等，1993）。然而，由于缺乏模型研究系统、易于检测的表型及其检测方法，关于这一重要过程的机制细节很少。细菌病毒 MS2 以其简单性而著称。 MS2是一种24nm二十面体病毒，仅由两种蛋白质组成：180个拷贝的外壳蛋白（Mr=13.7KDa）、一个拷贝的成熟蛋白A（Mr=44KDa）以及单链基因组RNA。因此，它是一个特征明确的遗传和生化系统（Golmoham madi 等，1993；Konig 等，2003；Ni 等，1995；Stonehouse 和 Stockley，1993；Stonehouse 等，1996；Valegard 等，1990；Valegard 等，1991；Valegard 等，1997； Valegard 等人，1986；van den Worm 等人，2006）。最近，我们的小组使用溶液中的小角度散射技术表明，在感染过程中，外壳会经历外壳特异性的厚度变化，我们假设这是由单一蛋白质 A 介导的（Kuzmanovic 等人，2006b）。尽管通过小角中子散射 (SANS) 测量的厚度变化是巨大的，在不存在 A 蛋白的情况下从 21A 变为 31A，但以前使用冷冻电镜或 X 射线晶体学并未观察到这些变化（Kuzmanovic 等人，2006b）（Golmohammadi 等人，1993；（Toropova 等人，2008）

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A virtually universal property of viruses is the requirement for the virus coat to make the transition from being an inert rigid protective outer coating to an activated dynamic particle capable of nucleic acid delivery during infection. This dynamic process requires conformational changes in the virus coat (Poranen, Daugelavicius, and Bamford, 2002) (Dryden et al., 1993; Endrich, Gehrig, and Gehrig, 1999; Fuller and Lee, 1992; Kirnbauer et al., 1993). However few mechanistic details are available about this essential process because of a lack of a model research system, an easily detectable phenotype and an assay for their detection. The bacterial virus MS2 is exceptional for its simplicity. MS2 is a 24nm icosahedral virus composed of only two proteins, 180 copies of coat protein(Mr=13.7KDa), a single copy of a maturation protein called A (Mr=44KDa) as well as a single stranded genomic RNA. As a result, it is a well characterized genetic and biochemical system (Golmoham madi et al., 1993; Konig et al., 2003; Ni et al., 1995; Stonehouse and Stockley, 1993; Stonehouse et al., 1996; Valegard et al., 1990; Valegard et al., 1991; Valegard et al., 1997; Valegard et al., 1986; van den Worm et al., 2006). Recently, our group has shown that the coat undergoes coat-specific changes in thickness during infection which we hypothesize are mediated by a single protein, A, using small angle scattering techniques in solution(Kuzmanovic et al., 2006b). Although, the change in thickness as measured by small angle neutron scattering (SANS) is dramatic, 21A to 31A in the absence A protein, these changes have not been observed previously using either cryo-EM or X-ray crystallography (Kuzmanovic et al., 2006b) (Golmohammadi et al., 1993; (Toropova et al., 2008)