Laboratori Nazionali Frascati, National Institute for Nuclear Physics (INFN-LNF), Via E. Fermi 54, 00044 Frascati, Italy.
Department of Physics, University of Rome 'La Sapienza', P.le A. Moro 2, 00185 Rome, Italy.
Int J Mol Sci. 2023 May 31;24(11):9550. doi: 10.3390/ijms24119550.
All coronaviruses are characterized by spike glycoproteins whose S1 subunits contain the receptor binding domain (RBD). The RBD anchors the virus to the host cellular membrane to regulate the virus transmissibility and infectious process. Although the protein/receptor interaction mainly depends on the spike's conformation, particularly on its S1 unit, their secondary structures are poorly known. In this paper, the S1 conformation was investigated for MERS-CoV, SARS-CoV, and SARS-CoV-2 at serological pH by measuring their Amide I infrared absorption bands. The SARS-CoV-2 S1 secondary structure revealed a strong difference compared to those of MERS-CoV and SARS-CoV, with a significant presence of extended β-sheets. Furthermore, the conformation of the SARS-CoV-2 S1 showed a significant change by moving from serological pH to mild acidic and alkaline pH conditions. Both results suggest the capability of infrared spectroscopy to follow the secondary structure adaptation of the SARS-CoV-2 S1 to different environments.
所有冠状病毒的特征是穗状糖蛋白，其 S1 亚基包含受体结合域（RBD）。RBD 将病毒锚定在宿主细胞膜上，以调节病毒的传染性和感染过程。尽管蛋白/受体相互作用主要取决于穗状的构象，特别是其 S1 单位，但它们的二级结构知之甚少。在本文中，通过测量酰胺 I 红外吸收带，在血清学 pH 值下研究了 MERS-CoV、SARS-CoV 和 SARS-CoV-2 的 S1 构象。与 MERS-CoV 和 SARS-CoV 相比，SARS-CoV-2 的 S1 二级结构显示出明显的差异，具有明显的伸展β-折叠。此外，SARS-CoV-2 S1 的构象通过从血清学 pH 值向温和酸性和碱性 pH 值条件移动而发生显著变化。这两个结果表明，红外光谱法能够跟踪 SARS-CoV-2 S1 的二级结构适应不同环境的能力。
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