Structural and molecular basis of the epistasis effect in enhanced affinity between SARS-CoV-2 KP.3 and ACE2

Cell Discovery, 30 December, 2024, DOI：https://doi.org/10.1038/s41421-024-00752-2

Structural and molecular basis of the epistasis effect in enhanced affinity between SARS-CoV-2 KP.3 and ACE2

Leilei Feng, Zhaoxi Sun, Yuchen Zhang, Fanchong Jian, Sijie Yang, Keely Xia, Lingling Yu, Jing Wang, Fei Shao, Xiangxi Wang & Yunlong Cao

Abstract

Recently, the SARS-CoV-2 KP.2-like (known as “FLiRT”) and KP.3 variants from the JN.1 family have become the dominant variants. KP.2 and KP.3 carry new F456L/R346T and F456L/Q493E mutations on the viral receptor-binding domain (RBD) of the Spike glycoprotein compared to JN.1, respectively (Fig. 1a, b). Mutations observed in these lineages, especially F456L and Q493E, are located on the interface between RBD and human ACE2 (hACE2) and are shown to affect the receptor-binding affinity and substantially escape the Class 1 neutralizing antibodies (NAbs).

文章链接：https://www.nature.com/articles/s41421-024-00752-2