小柯机器人

近日，中国生物研究院李启明等研究人员合作发现，突变RSV F蛋白的灵活区域可以稳定预融合构象。这一研究成果发表在2024年9月27日出版的国际学术期刊《科学》上。

据研究人员介绍，呼吸道合胞病毒（RSV）融合（F）糖蛋白在其预融合（pre-F）构象中具有很高的免疫原性。然而，该蛋白不稳定，其构象必须得到稳定，才能有效地作为疫苗中的免疫原。

Title: Mutating a flexible region of the RSV F protein can stabilize the prefusion conformation

Author: Yu Liang, Shuai Shao, Xin Yu Li, Zi Xin Zhao, Ning Liu, Zhao Ming Liu, Fu Jie Shen, Hao Zhang, Jun Wei Hou, Xue Feng Zhang, Yu Qin Jin, Li Fang Du, Xin Li, Jing Zhang, Ji Guo Su, Qi Ming Li

Issue&Volume: 2024-09-27

Abstract: The respiratory syncytial virus (RSV) fusion (F) glycoprotein is highly immunogenic in its prefusion (pre-F) conformation. However, the protein is unstable, and its conformation must be stabilized for it to function effectively as an immunogen in vaccines. We present a mutagenesis strategy to arrest the RSV F protein in its pre-F state by blocking localized changes in protein structure that accompany large-scale conformational rearrangements. We generated a series of mutants and screened them in vitro to assess their potential for forming a stable pre-F. In animals, the immunogenicity of a representative mutant F protein, with a conformation confirmed by cryo–electron microscopy, elicited levels of neutralizing antibodies and protection against RSV-induced lung damage that were comparable to those of DS-Cav1, a pre-F used in a licensed vaccine.

DOI: adp2362

Source: https://www.science.org/doi/10.1126/science.adp2362