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首页> 外文期刊>Journal of Molecular Biology >Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry.
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Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry.

机译：通过高分辨率质谱鉴定HIV-1衣壳蛋白装配中的新相互作用。

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摘要

The pleomorphic nature of the immature and mature HIV-1 virions has made it difficult to characterize intersubunit interactions using traditional approaches. While the structures of isolated domains are known, the challenge is to identify intersubunit interactions and thereby pack these domains into supramolecular structures. Using high-resolution mass spectrometry, we have measured the amide hydrogen exchange protection factors for the soluble capsid protein (CA) and CA assembled in vitro. Comparison of the protection factors as well as chemical crosslinking experiments has led to a map of the subunit/subunit interfaces in the assembled tubes. This analysis provides direct biochemical evidence for the homotypic N domain and C domain interactions proposed from cryo-electron microscopy image reconstruction of CA tubes. Most significantly, we have identified a previously unrecognized intersubunit N domain-C domain interaction. The detection of this interaction reconciles previously discrepant biophysicaland genetic data.
机译：不成熟和成熟的HIV-1病毒体的多态性使其很难用传统方法表征亚基间的相互作用。虽然分离的结构域的结构是已知的，但是挑战在于识别亚基间相互作用，从而将这些结构域包装成超分子结构。使用高分辨率质谱，我们已经测量了可溶性衣壳蛋白（CA）和体外组装的CA的酰胺氢交换保护因子。保护因子的比较以及化学交联实验导致了组装管中亚基/亚基界面的图谱。该分析为CA管的低温电子显微镜图像重建提出的同型N域和C域相互作用提供了直接的生化证据。最重要的是，我们确定了以前无法识别的亚基间N域-C域相互作用。这种相互作用的检测使以前不一致的生物物理遗传数据协调一致。

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