Wharton S A, Skehel J J, Wiley D C
Virology. 1986 Feb;149(1):27-35. doi: 10.1016/0042-6822(86)90083-8.
A resonance energy transfer assay of membrane fusion developed by P. S. Uster and D. W. Deamer (Biochemistry 24, 1-8 (1985)) was used in a study of influenza haemagglutinin-mediated fusion. The characteristics of fusion and haemolysis by X-31 (H3N2) virus, a number of mutants of X-31 which fuse membranes at higher pH, and purified haemagglutinins released from virus particles either by detergent dissociation or by bromelain digestion were compared with particular regard to pH and temperature dependence. The finding that membrane fusion activity, haemolysis, and changes in haemagglutinin conformation covary with pH and temperature provide support for the role of haemagglutinin in fusion and are discussed in relation to the stability of its structure.
P. S. 乌斯特和D. W. 迪默(《生物化学》24卷,第1 - 8页(1985年))开发的一种用于膜融合的共振能量转移测定法被用于流感血凝素介导的融合研究。比较了X - 31(H3N2)病毒、一些在较高pH值下融合膜的X - 31突变体以及通过去污剂解离或菠萝蛋白酶消化从病毒颗粒中释放的纯化血凝素的融合和溶血特性,特别关注了pH值和温度依赖性。膜融合活性、溶血以及血凝素构象变化随pH值和温度共同变化这一发现为血凝素在融合中的作用提供了支持,并结合其结构稳定性进行了讨论。