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利用纳米红外光谱成像技术探测单包膜病毒颗粒的结构变化。

Probing structural changes in single enveloped virus particles using nano-infrared spectroscopic imaging.

机构信息

Department of Physics and Astronomy, University of Georgia, Athens, Georgia, United States of America.

Department of Physics and Astronomy, Georgia State University, Atlanta, Georgia, United States of America.

出版信息

PLoS One. 2018 Jun 12;13(6):e0199112. doi: 10.1371/journal.pone.0199112. eCollection 2018.

DOI:10.1371/journal.pone.0199112
PMID:29894493
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5997350/
Abstract

Enveloped viruses, such as HIV, Ebola and Influenza, are among the most deadly known viruses. Cellular membrane penetration of enveloped viruses is a critical step in the cascade of events that lead to entry into the host cell. Conventional ensemble fusion assays rely on collective responses to membrane fusion events, and do not allow direct and quantitative studies of the subtle and intricate fusion details. Such details are accessible via single particle investigation techniques, however. Here, we implement nano-infrared spectroscopic imaging to investigate the chemical and structural modifications that occur prior to membrane fusion in the single archetypal enveloped virus, influenza X31. We traced in real-space structural and spectroscopic alterations that occur during environmental pH variations in single virus particles. In addition, using nanospectroscopic imaging we quantified the effectiveness of an antiviral compound in stopping viral membrane disruption (a novel mechanism for inhibiting viral entry into cells) during environmental pH variations.

摘要

包膜病毒,如艾滋病毒、埃博拉病毒和流感病毒,是已知最致命的病毒之一。包膜病毒对细胞膜的穿透是导致进入宿主细胞的一系列事件中的关键步骤。传统的整体融合分析依赖于对膜融合事件的集体反应,并且不允许对微妙而复杂的融合细节进行直接和定量的研究。然而,通过单颗粒研究技术可以获得这些细节。在这里,我们实施纳米红外光谱成像来研究在单个原型包膜病毒流感 X31 中发生的膜融合之前发生的化学和结构修饰。我们在单病毒颗粒中追踪了在环境 pH 值变化过程中发生的结构和光谱改变。此外,使用纳米光谱成像,我们定量了一种抗病毒化合物在环境 pH 值变化过程中阻止病毒膜破坏的效果(一种抑制病毒进入细胞的新机制)。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/438e1e6260eb/pone.0199112.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/4c57242deca4/pone.0199112.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/73f5ec7e1d6c/pone.0199112.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/e260d0214b15/pone.0199112.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/aacac1542ce7/pone.0199112.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/6a2683231c27/pone.0199112.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/438e1e6260eb/pone.0199112.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/4c57242deca4/pone.0199112.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/73f5ec7e1d6c/pone.0199112.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/e260d0214b15/pone.0199112.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/aacac1542ce7/pone.0199112.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/6a2683231c27/pone.0199112.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/09c1/5997350/438e1e6260eb/pone.0199112.g006.jpg

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