Structure and function of a pair of non-competing monoclonal antibodies against Langya henipavirus attachment glycoprotein

作者：Wenting Li, Songyue Wu, Qi Gui, Congcong Liu, Bing Zhou, Yan Hu, Yuehong Sun, Qing Fan, Yuzheng Zhou, Huimin Guo, Shilong Tang, Xiangyang Ge, Bin Ju, Renhong Yan, Zheng Zhang · 发表于：Cell Reports · 年份：2025 · DOI：10.1016/j.celrep.2025.116407 · 被引用次数：6 · 研究领域：Virology and Viral Diseases、Viral Infections and Vectors、Plant Virus Research Studies

Langya henipavirus (LayV) is a zoonotic Parahenipavirus (Para-HNV) identified in recent years, discovered via surveillance of febrile patients with recent animal exposure in eastern China. The attachment glycoprotein (G) of HNV is critical for host cell entry and a key immune target. However, LayV-G exhibits notable antigenic differences from G of highly pathogenic bat-borne Hendra virus (HEV) and Nipah virus (NiV), implying vaccines or antibody therapies developed against HeV/NiV-G might be ineffective against LayV. Here, we immunize mice with LayV-G ectodomain and isolate a panel of LayV-G-targeting monoclonal antibodies (mAbs). We characterize two potent mAbs with pronounced crystallizable fragment (Fc)-mediated antiviral function and determine their cryo-electron microscopy (cryo-EM) structure binding to distinct epitopes of LayV-G head domain at a resolution of 2.92 Å, revealing antibody recognition mechanisms and potential conformational dynamics of LayV-G. Overall, our study defines two function-related epitopes of LayV-G, laying the foundation for therapeutic antibody development and vaccine design.