Binding of cholesterol and inhibitory peptide derivatives with the fusogenic hydrophobic sequence of F-glycoprotein of HVJ (Sendai virus): possible implication in the fusion reaction.
Binding of cholesterol and inhibitory peptide derivatives with the fusogenic hydrophobic sequence of F-glycoprotein of HVJ (Sendai virus): possible implication in the fusion reaction.
复制标题
胆固醇和抑制肽衍生物与 HVJ（仙台病毒）F-糖蛋白的融合疏水序列的结合：融合反应中的可能含义。
DOI：
10.1021/bi00404a035
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
A. Asano
中科院分区：
文献类型：
--
作者：
K. Asano;A. Asano
通过与[3H]胆固醇的结合竞争，研究了甾醇和相关化合物与HVJ（仙台病毒）的纯化F蛋白（融合蛋白）结合的特异性。在该结合中发现需要胆固醇或A/B环反式结构并且不需要3-羟基。使用纯化的蛋白质和病毒粒子研究了 125I 标记的 Z-Phe-Tyr（一种病毒膜-细胞膜融合的抑制肽）的结合。 F-蛋白和病毒粒子显示出与肽的特异性结合，而血凝素和神经氨酸酶蛋白的结果为阴性。嗜热菌蛋白酶截短的 F 蛋白（一种从 F1 亚基 N 端去除 2.5 kDa 片段且无融合活性的 F 蛋白衍生物）表现出与胆固醇和抑制肽的结合能力显着降低。因此，之前被指定为融合的 N 端疏水序列似乎是这些分子的结合位点。支持这一点的是，胆固醇与 F 蛋白的结合受到 Z-Phe-Tyr 和其他融合抑制肽的抑制，而不受非融合抑制性 Z-Gly-Phe 的影响。这些结果的讨论涉及以下概念：F 蛋白的 F1 亚基的 N 末端部分与靶细胞膜中的胆固醇的结合促进融合反应。
Specificity of the binding of sterols and related compounds with purified F-protein (fusion protein) of the HVJ (Sendai virus) was studied by binding competition with [3H]cholesterol. Requirement for cholesterol or the A/B ring trans structure and nonrequirement for the 3-hydroxyl group were found in this binding. Binding of 125I-labeled Z-Phe-Tyr, an inhibitory peptide of viral membrane-cell membrane fusion, was studied by using purified proteins and virions. F-Protein and virions showed a specific binding with the peptide, whereas the result was negative with hemagglutinin and neuraminidase protein. Thermolysin-truncated F-protein (an F-protein derivative deprived of a 2.5-kDa fragment from the N-terminal of the F1 subunit and without fusogenic activity) exhibited a considerably diminished binding ability both to cholesterol and to inhibitory peptides. Therefore, the N-terminal hydrophobic sequence that was previously assigned as fusogenic seems to be the binding site of these molecules. In support of this, the binding of cholesterol with F-protein was inhibited by Z-Phe-Tyr and other fusion inhibitory peptides, whereas it was not affected with non-fusion-inhibitory Z-Gly-Phe. These results are discussed in relation to the notion that the binding of the N-terminal portion of the F1 subunit of F-protein with cholesterol in the target cell membranes facilitates the fusion reaction.
仙台F蛋白的融合相关疏水结构域可以穿过大肠杆菌的细胞质膜。
DOI：
10.1073/pnas.83.14.5091
发表时间：
1986
影响因子：
11.1
作者：
Davis,NG;Hsu,MC
通讯作者：
Hsu,MC
使用病毒基因的 cDNA 克隆和融合蛋白的生物学重要区域的序列分析仙台病毒 mRNA。
DOI：
10.1073/pnas.81.24.7732
发表时间：
1984
影响因子：
11.1
作者：
Hsu,M;Choppin,PW
通讯作者：
Choppin,PW
仙台病毒融合蛋白（f）的激活涉及随着新疏水区域的暴露而发生的构象变化。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Hsu,M;Scheid,A;Choppin,PW
通讯作者：
Choppin,PW