通过与N螺旋嵌合体异源寡聚化有效捕获HIV-1包膜蛋白。
Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera.
作者信息
Ou Wu, Silver Jonathan
机构信息
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Building 4, Bethesda, MD 20892, USA.
出版信息
Retrovirology. 2005 Aug 10;2:51. doi: 10.1186/1742-4690-2-51.
BACKGROUND
The N-heptad repeat region of the HIV-1 Transmembrane Envelope protein is a trimerization domain that forms part of a "six helix bundle" crucial to Envelope-mediated membrane fusion. N-heptad repeat peptides have been used as extracellular reagents to inhibit virus fusion.
RESULTS
When expressed intracellularly with wild-type HIV-1 Envelope protein, the N-heptad repeat domain efficiently hetero-oligomerized with Envelope and trapped it in the endoplasmic reticulum or early Golgi, as indicated by lack of transport to the cell surface, absent proteolytic processing, and aberrant glycosylation.
CONCLUSION
Post-translational processing of HIV Envelope is very sensitive to an agent that binds to the N-heptad repeat during synthesis, suggesting that it might be possible to modify drugs that bind to this region to have transport-blocking properties.
背景
HIV-1跨膜包膜蛋白的N-七聚体重复区域是一个三聚化结构域，它构成了对包膜介导的膜融合至关重要的“六螺旋束”的一部分。N-七聚体重复肽已被用作细胞外试剂来抑制病毒融合。
结果
当与野生型HIV-1包膜蛋白在细胞内共表达时，N-七聚体重复结构域与包膜高效异源寡聚化，并将其截留在内质网或早期高尔基体中，这表现为无法转运到细胞表面、缺乏蛋白水解加工以及糖基化异常。
结论
HIV包膜的翻译后加工对合成过程中与N-七聚体重复序列结合的试剂非常敏感，这表明有可能对结合该区域的药物进行修饰，使其具有转运阻断特性。
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