生物
疱疹病毒糖蛋白B
糖蛋白
膜糖蛋白
单纯疱疹病毒
突变体
跨膜蛋白
生物化学
肽序列
跨膜结构域
病毒包膜
氨基酸
分子生物学
细胞生物学
病毒进入
病毒
病毒复制
病毒学
基因
受体
作者
L Rasile,Kaushik Ghosh,Kanakatte Raviprakash,Hara P. Ghosh
出处
期刊:Journal of Virology
[American Society for Microbiology]
日期:1993-08-01
卷期号:67 (8): 4856-4866
被引量:42
标识
DOI:10.1128/jvi.67.8.4856-4866.1993
摘要
The gB glycoprotein of herpes simplex virus type 1 is involved in viral entry and fusion and contains a predicted membrane-anchoring sequence of 69 hydrophobic amino acids, which can span the membrane three times, near the carboxy terminus. To define the membrane-anchoring sequence and the role of this hydrophobic stretch, we have constructed deletion mutants of gB-1, lacking one, two, or three predicted membrane-spanning segments within the 69 amino acids. Expression of the wild-type and mutant glycoproteins in COS-1 cells show that mutant glycoproteins lacking segment 3 (amino acids 774 to 795 of the gB-1 protein) were secreted from the cells. Protease digestion and alkaline extraction of microsomes containing labeled mutant proteins further showed that segment 3 was sufficient for stable membrane anchoring of the glycoproteins, indicating that this segment may specify the transmembrane domain of the gB glycoprotein. Also, the mutant glycoproteins containing segment 3 were localized in the nuclear envelop, which is the site of virus budding. Deletion of any of the hydrophobic segments, however, affected the intracellular transport and processing of the mutant glycoproteins. The mutant glycoproteins, although localized in the nuclear envelope, failed to complement the gB-null virus (K082). These results suggest that the carboxy-terminal hydrophobic region contains essential structural determinants of the functional gB glycoprotein.
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