Integral Molecular, Inc., Philadelphia, PA 19104, United States.
Virology. 2012 Nov 25;433(2):401-9. doi: 10.1016/j.virol.2012.08.023. Epub 2012 Sep 17.
To better understand how detergents disrupt enveloped viruses, we monitored the biophysical stability of murine leukemia virus (MLV) virus-like particles (VLPs) against a panel of commonly used detergents using real-time biosensor measurements. Although exposure to many detergents, such as Triton X-100 and Empigen, results in lysis of VLP membranes, VLPs appeared resistant to complete membrane lysis by a significant number of detergents, including Tween 20, Tween 80, Lubrol, and Saponin. VLPs maintained their structural integrity after exposure to Tween 20 at concentrations up to 500-fold above its CMC. Remarkably, VLPs containing immature cores composed of unprocessed (uncleaved) Gag polyprotein were significantly more resistant to detergent lysis than VLPs with mature cores. Although the maturity of retroviral Gag is known to influence the stability of the protein core structure itself, our studies suggest that the maturity of the Gag core also influences the stability of the lipid bilayer surrounding the core.
为了更好地了解清洁剂如何破坏包膜病毒，我们使用实时生物传感器测量法，监测了一系列常用清洁剂对鼠白血病病毒（MLV）病毒样颗粒（VLPs）的生物物理稳定性。尽管许多清洁剂（如 Triton X-100 和 Empigen）的暴露会导致 VLP 膜的裂解，但 VLPs 似乎对许多清洁剂（包括 Tween 20、Tween 80、Lubrol 和 Saponin）的完全膜裂解具有抗性。VLPs 在 Tween 20 浓度高达其 CMC 以上 500 倍的情况下仍保持其结构完整性。值得注意的是，含有未成熟核心（未加工（未切割）Gag 多聚蛋白）的 VLPs 比具有成熟核心的 VLPs 对清洁剂裂解的抵抗力要强得多。尽管已知逆转录病毒 Gag 的成熟度会影响蛋白核心结构本身的稳定性，但我们的研究表明，Gag 核心的成熟度也会影响围绕核心的脂质双层的稳定性。
