BACTERIOPHAGE EPSILON 15

这个子项目是许多研究子项目中的一个 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。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 噬菌体ε 15是感染人/动物病原体肠道沙门氏菌Anatum血清型的通用转导噬菌体。已经研究了Ep 15识别和结合O-抗原的能力以及其在溶原状态下改变宿主脂多糖的能力。负责O-抗原识别的病毒蛋白是尾刺蛋白。该病毒体含有至少6种结构蛋白和一个约40 kb的已知序列的dsDNA基因组。在序列水平上，结构蛋白最接近伯克霍尔德氏菌的Bcep，伯克霍尔德氏菌是一种影响囊性纤维化患者的人类病原体。病毒粒子结构蛋白和染色体一起形成一个质量约为66兆道尔顿，直径约为650埃的粒子。乔恩·金的实验室已经使用质谱方法来鉴定那些编码病毒体结构蛋白的开放阅读框架。这种病毒的结构将揭示结构蛋白的排列，特别是那些更直接参与附着宿主和DNA进入细胞质的亚基的构型。目前正在进行一种遗传学方法来分离病毒结构蛋白中的琥珀突变体。在用这些突变体噬菌体感染期间形成的大分子印迹将被纯化并通过重建成像。这些突变体噬菌体还将作为用于成像病毒与宿主表面的脂多糖和受体蛋白之间的相互作用的试剂。

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. 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 650¿ . 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.