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

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 病毒的一个几乎普遍的性质是要求病毒外壳从惰性的刚性保护外层转变为能够在感染期间运送核酸的激活的动态粒子。这一动态过程需要病毒外壳的构象变化(Poranen，Dugelavicius和Bamford，2002)(Dryden等人，1993；Endrich，Gehrig和Gehrig，1999；Fuller和Lee，1992；Kirnbauer等人，1993)。然而，由于缺乏模型研究系统、易于检测的表型和检测它们的方法，关于这一基本过程的机制细节很少。细菌病毒MS2因其简单性而与众不同。MS2是一种24 nm的二十面体病毒，由两种蛋白质、180个拷贝的外壳蛋白(MR=13.7 KDa)、一个称为A的成熟蛋白(MR=44 KDa)以及一个单链基因组RNA组成。因此，它是一个具有良好特征的遗传和生化系统(Golmoham Madi等人，1993；Konig等人，2003；Ni等人，1995；Stonehouse and Stockley，1993；Stonehouse等人，1996；Valegard等人，1990；Valegard等人，1991；Valegard等人，1997；Valegard等人，1986；van den Worm等人，2006)。最近，我们的团队已经证明，在感染期间，被毛经历了特定于被毛的厚度变化，我们假设这是由一种单一的蛋白质A介导的，在溶液中使用小角度散射技术(Kuzmanovic等人，2006b)。虽然，通过小角中子散射(SANS)测量的厚度变化是戏剧性的，在没有A蛋白的情况下，从21A到31A，但这些变化以前没有使用冷冻-EM或X射线结晶学观察到(Kuzmanovic等人，2006b)(Golmohammadi等人，1993；(Toropova等人，2008年)

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)