Department of Chemistry, Pennsylvania State University, University Park, PA, United States.
Department of Chemistry, Pennsylvania State University, University Park, PA, United States; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, United States; The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA, United States.
Curr Opin Struct Biol. 2024 Jun;86:102787. doi: 10.1016/j.sbi.2024.102787. Epub 2024 Mar 7.
X-ray crystallography and cryo-electron microscopy have enabled the determination of structures of numerous viruses at high resolution and have greatly advanced the field of structural virology. These structures represent only a subset of snapshot end-state conformations, without describing all conformational transitions that virus particles undergo. Allostery plays a critical role in relaying the effects of varied perturbations both on the surface through environmental changes and protein (receptor/antibody) interactions into the genomic core of the virus. Correspondingly, allostery carries implications for communicating changes in genome packaging to the overall stability of the virus particle. Amide hydrogen/deuterium exchange mass spectrometry (HDXMS) of whole viruses is a powerful probe for uncovering virus allostery. Here we critically discuss advancements in understanding virus dynamics by HDXMS with single particle cryo-EM and computational approaches.
X 射线晶体学和低温电子显微镜使许多病毒的结构能够以高分辨率确定，并极大地推动了结构病毒学领域的发展。这些结构仅代表快照终态构象的一个子集，并未描述病毒颗粒经历的所有构象转变。变构作用在通过环境变化和蛋白质（受体/抗体）相互作用将各种扰动的影响传递到病毒基因组核心方面起着关键作用。相应地，变构作用对基因组包装的变化与病毒颗粒整体稳定性的传递具有重要意义。完整病毒的酰胺氢/氘交换质谱（HDXMS）是揭示病毒变构作用的有力探针。在这里，我们通过单颗粒冷冻电镜和计算方法，批判性地讨论了通过 HDXMS 理解病毒动力学的进展。
