BACTERIOPHAGE EPSILON 15

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 噬菌体Epsilon 15是一种感染人/动物的全面性转导噬菌体 病原菌肠炎沙门氏菌血清型。人们对Epsilon 15进行了研究，因为它具有 识别和结合O-抗原及其改变宿主内毒素的能力 溶源状态。负责识别O抗原的病毒蛋白是尾钉蛋白。 该病毒粒子含有至少6种结构蛋白和大约40kb的dsdna。 已知序列的基因组。在序列水平上，最接近的结构蛋白 与伯克霍尔德氏菌的Bcep噬菌体相似，伯克霍尔德氏菌是一种影响囊性纤维化的人类病原体 病人。病毒粒子结构蛋白和染色体一起形成一个具有 质量约为66兆吨，直径约为6500？乔恩·金的实验室 使用质谱学方法鉴定编码病毒粒子的开放阅读框 结构蛋白。这种病毒的结构将揭示出结构的排列 蛋白质，特别是那些更直接参与的亚基的构型 附着在宿主上，并通过DNA进入细胞质。一种遗传方法现在是 正在分离病毒结构蛋白中的琥珀突变体。大分子 在感染这些突变噬菌体期间形成的亚组分将被提纯和成像 通过重建。这些突变的噬菌体也将作为显像剂 病毒与病毒表面脂多糖和受体蛋白的相互作用 主持人。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Bacteriophage Epsilon15 is a generalized transducing phage infecting the human/animal pathogen Salmonella enterica serovar Anatum. Epsilon 15 has been studied for its ability to recognize and bind O-antigen as well as its capacity to alter host lipopolysaccharide in the lysogenic state. The viral protein responsible for O-antigen recognition is the tailspike protein. The virion contains at least six structural proteins and an approximately 40 kb dsDNA genome of known sequence. At the sequence level, the structural proteins most closely resemble the Bcep phages of Burkholderia, a human pathogen affecting cystic fibrosis patients. The virion structural proteins and chromosome together make a particle with a mass of approximately 66 Megadaltons and a diameter of roughly 6500 ¿. Jon King's lab has used mass spectrometric methods to identify those open reading frames encoding virion structural proteins. The structure of this virus will reveal the arrangement of structural proteins and, in particular, the configuration of those subunits more directly involved in attachment to the host and passage of DNA into the cytoplasm. A genetic approach is now underway to isolate amber mutants in virus structural proteins. Macromolecular subassemblies formed during infections with these mutant phage will be purified and imaged by reconstruction. These mutant phage will also serve as reagents for imaging the interactions between virus and lipopolysaccharide and receptor proteins at the surface of the host.