BACTERIOPHAGE EPSILON 15

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。次级项目的主要支助 子项目的主要研究者可能是由其他来源提供的， 包括其它NIH来源。 为子项目列出的总成本可能 表示子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 噬菌体ε 15是感染人/动物的通用转导噬菌体 病原体肠道沙门氏菌Anatum血清型Epoxy 15已经被研究了它的能力 识别并结合O-抗原以及其改变宿主脂多糖的能力， 溶原状态负责O-抗原识别的病毒蛋白是尾刺蛋白。 该病毒粒子含有至少6种结构蛋白和一个约40 kb的双链DNA 已知序列的基因组。在序列水平上，结构蛋白质最接近 类似于伯克霍尔德氏菌的Bcep，伯克霍尔德氏菌是一种影响囊性纤维化的人类病原体 患者病毒体结构蛋白和染色体一起形成一个具有 质量约为66兆道尔顿，直径约为6500磅。乔恩·金的实验室 用质谱方法鉴定那些编码病毒体的开放阅读框 结构蛋白这种病毒的结构将揭示结构的排列 蛋白质，特别是那些更直接参与蛋白质合成的亚基的构型， 附着于宿主并将DNA传递到细胞质中。一种遗传学方法现在 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噬菌体将被纯化和成像 通过重建。这些突变体噬菌体也将作为成像试剂， 病毒与脂多糖和受体蛋白之间的相互作用 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.