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

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH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 中心，不一定是研究者的机构。 病毒的一个几乎普遍的性质是需要病毒外壳从惰性的刚性保护性外涂层转变为能够在感染期间递送核酸的活化的动态颗粒。 该动态过程需要病毒外壳中的构象变化（Poranen，Daugelavicius和Bamford，2002）（德莱登等人，1993; Endrich，Gehrig和Gehrig，1999; Fuller和Lee，1992; Kirnbauer等人，1993年）。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测定法，关于这个基本过程的机制细节很少。细菌病毒MS 2因其简单性而与众不同。MS 2是一种24 nm的二十面体病毒，仅由两种蛋白质组成，180个拷贝的外壳蛋白（Mr=13.7KDa），一个单拷贝的成熟蛋白A（Mr= 44 KDa）以及单链基因组RNA。因此，它是一个充分表征的遗传和生物化学系统（Golmohammadi等人，1993; Konig等人，2003; Ni等人，1995; Stonehouse和Stockley，1993; Stonehouse等人，1996; Valegard等人，1990; Valegard等人，1991; Valegard等人，1997; Valegard等人，1986;货车den Worm等人，2006年）。最近，我们的小组已经表明，在感染期间，利用溶液中的小角散射技术，被毛经历了被毛特异性的厚度变化，我们假设这是由单一蛋白A介导的（Kuzbovic等人，2006年b）。虽然，通过小角中子散射（SANS）测量的厚度变化是显著的，在不存在A蛋白的情况下为21 A至31 A，但是这些变化先前使用冷冻EM或X射线晶体学都没有观察到（Kuzbovic等人，2006 b）（Golmohammadi等人，1993年;（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)