膜锚定结构域和细胞质结构域对水疱性口炎病毒糖蛋白G融合活性的影响。
Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G.
作者信息
Odell D, Wanas E, Yan J, Ghosh H P
机构信息
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
出版信息
J Virol. 1997 Oct;71(10):7996-8000. doi: 10.1128/JVI.71.10.7996-8000.1997.
Abstract
Chimeric proteins in which the transmembrane anchoring sequence (TM) or both the TM and the cytoplasmic tail (CT) of vesicular stomatitis virus glycoprotein G were replaced with corresponding domains of viral or cellular integral membrane proteins were used to examine the influence of these domains on acidic-pH-induced membrane fusion by G protein. The TM and CT of G were also replaced with the lipid anchor glycosylphosphatidylinositol. Hybrids containing foreign TM or TM and CT sequences were fusogenic at acidic pH but glycosylphosphatidylinositol-anchored G was nonfusogenic at acidic pH. The results suggest that the fusogenic activity of G protein requires membrane anchoring by a hydrophobic peptide sequence and the specific amino acid sequence of the TM has no influence on fusogenic activity.
摘要
用嵌合蛋白来研究水泡性口炎病毒糖蛋白G的跨膜锚定序列（TM）或TM与胞质尾（CT）二者被病毒或细胞整合膜蛋白的相应结构域取代后，这些结构域对G蛋白酸性pH诱导的膜融合的影响。G的TM和CT也被脂质锚定糖基磷脂酰肌醇取代。含有外源TM或TM与CT序列的杂种在酸性pH下具有融合活性，但糖基磷脂酰肌醇锚定的G在酸性pH下无融合活性。结果表明，G蛋白的融合活性需要通过疏水肽序列进行膜锚定，且TM的特定氨基酸序列对融合活性没有影响。
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