The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment

Intact influenza A virions were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the label in the matrix protein M1 was analyzed to determine the in situ accessibility of its tryptic fragments. These data were combined with the previously reported x-ray crystal structure of the M1 fragment 2–158 [Sha, B. & Luo, M. (1997) Nat. Struct. Biol. 4, 239–244] and the predicted topology of the C domain (159–252) to propose a model of M1 arrangement in the virus particle.

研究团队将完整的甲型流感病毒体经热活化氚原子轰击后，对基质蛋白M1内标记物的分子内分布进行分析，以此确定其胰蛋白酶水解片段的原位可及性。本研究将上述实验数据与此前已报道的M1片段2–158的X射线晶体结构[Sha, B. & Luo, M. (1997) Nat. Struct. Biol. 4, 239–244]以及C端结构域（159–252）的预测拓扑结构相结合，提出了M1蛋白在病毒颗粒中的排布模型。