Carbonell X, Villaverde A
Institut de Biologia Fonamental, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Gene. 1996 Oct 17;176(1-2):225-9. doi: 10.1016/0378-1119(96)00255-7.
The tailspike protein (TSP) of Salmonella typhimurium P22 bacteriophage is a multifunctional homotrimer, 6 copies of which are non-covalently attached to the capsid to form the virion tail in the last reaction of phage assembly. An antigenic peptide of foot-and-mouth disease virus (FMDV), aa 134-156 of protein VP1, has been joined to the carboxy terminus of TSP, and produced as a fusion protein in Escherichia coli directed by the trp promoter. The resulting fusion protein is soluble, stable, non-toxic, and can be easily purified by standard procedures. Moreover, both the endorhamnosidase and capsid assembly activities of the TSP are conserved, permitting the fusion protein to reconstitute infectious viruses by in vitro association with tailless particles. In both free TSP and P22 chimeric virions, the foreign peptide is solvent-exposed and highly antigenic, indicating that P22 TSP could be an appropriate carrier protein for multimeric peptide display.
鼠伤寒沙门氏菌P22噬菌体的尾钉蛋白（TSP）是一种多功能同三聚体，在噬菌体组装的最后反应中，其6个拷贝非共价连接到衣壳上以形成病毒粒子尾部。口蹄疫病毒（FMDV）的一个抗原肽，即VP1蛋白的第134 - 156位氨基酸，已连接到TSP的羧基末端，并在色氨酸启动子的指导下在大肠杆菌中作为融合蛋白产生。所得融合蛋白可溶、稳定、无毒，并且可以通过标准程序轻松纯化。此外，TSP的内鼠李糖苷酶和衣壳组装活性均得以保留，使得融合蛋白能够通过在体外与无尾颗粒结合来重建感染性病毒。在游离的TSP和P22嵌合病毒粒子中，外源肽均暴露于溶剂中且具有高度抗原性，这表明P22 TSP可能是用于多聚体肽展示的合适载体蛋白。
