Kaminaka S, Imamura Y, Shingu M, Kitagawa T, Toyoda T
Department of Virology, Kurume University School of Medicine, Fukuoka, Japan.
J Virol Methods. 1999 Feb;77(2):117-23. doi: 10.1016/s0166-0934(98)00153-0.
The structural comparison of bovine enterovirus MZ468 strain before and after the heat treatment was studied by ultraviolet resonance Raman (UVRR) spectra excited at both 235 and 251 nm. The difference between full, heated full and purified empty particles, which were expected as an in vitro model of uncoating, were demonstrated. At 235 nm excitation, the Raman bands of the capsid protein dominated in all the UVRR spectra. The UVRR spectra of the empty particles exhibited non-homogenious broadening for tryptophan W3 band and W7 Fermi doublet bands, which were characteristics of hydrophobic environment, when compared with those of the full particles. The results indicates that some Trp indole rings of the full particles were packaged inside the viral capsids and not strained by virion assembly. On the other hand, the Raman bands assigned to guanine residues of the single stranded-RNA genome were enhanced strongly in the 251-nm excited UVRR spectrum. The spectral differences between the packaged (full particles) and the unpackaged virions (heated full particles) indicates that some guanine residues had strong hydrogen bonds in the full particles.
通过在235和251 nm激发的紫外共振拉曼（UVRR）光谱研究了热处理前后牛肠道病毒MZ468株的结构比较。展示了完整、加热后的完整和纯化空颗粒之间的差异，这些差异有望作为脱壳的体外模型。在235 nm激发下，衣壳蛋白的拉曼带在所有UVRR光谱中占主导地位。与完整颗粒相比，空颗粒的UVRR光谱显示色氨酸W3带和W7费米双峰带呈现非均匀展宽，这是疏水环境的特征。结果表明，完整颗粒的一些色氨酸吲哚环被包裹在病毒衣壳内部，并且不受病毒粒子组装的影响。另一方面，在251 nm激发的UVRR光谱中，分配给单链RNA基因组鸟嘌呤残基的拉曼带强烈增强。包装的（完整颗粒）和未包装的病毒粒子（加热后的完整颗粒）之间的光谱差异表明，完整颗粒中的一些鸟嘌呤残基具有很强的氢键。
