Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Napoli, Italy.
Biochemistry. 2012 Apr 10;51(14):3121-8. doi: 10.1021/bi201589m. Epub 2012 Mar 23.
Glycoprotein H (gH) of the herpes simplex virus type 1 is involved in the complex mechanism of membrane fusion of the viral envelope with host cells. The virus requires four glycoproteins (gB, gD, gH, gL) to execute fusion and the role played by gH remains mysterious. Mutational studies have revealed several regions of gH ectodomain required for fusion and identified the segment from amino acid 625 to 644 as the most fusogenic region. Here, we studied the behavior in a membrane-mimicking DPC micellar environment of a peptide encompassing this region (gH625-644) and determined its NMR solution structure and its orientation within the micelles.
单纯疱疹病毒 1 型糖蛋白 H (gH) 参与病毒包膜与宿主细胞融合的复杂机制。该病毒需要四种糖蛋白（gB、gD、gH、gL）来执行融合，而 gH 所扮演的角色仍然神秘。突变研究揭示了 gH 外域中融合所必需的几个区域，并确定了从氨基酸 625 到 644 的片段是最具融合性的区域。在这里，我们研究了包含该区域的肽（gH625-644）在模拟细胞膜的 DPC 胶束环境中的行为，并确定了其 NMR 溶液结构及其在胶束中的取向。
