9LEO

LayV-G Head in complex of LayG-1069 and LayG-1133

Summary for 9LEO

• Entry DOI: 10.2210/pdb9leo/pdb
• EMDB information: 63031
• Descriptor: LayG-1069 heavy chain, LayG-1069 light chain, LayG-1133 heavy chain, ... (5 entities in total)
• Functional Keywords: complex, virus protein, antibody, glycoprotein, henipa virus, viral protein-immune system complex, viral protein/immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 5
• Total formula weight: 144627.32

Authors

Yan, R.H.,Wu, S.Y. (deposition date: 2025-01-07, release date: 2025-10-01, Last modification date: 2026-04-15)

Primary citation

Li, W.,Wu, S.,Gui, Q.,Liu, C.,Zhou, B.,Yan, H.,Sun, Y.,Fan, Q.,Zhou, Y.,Guo, H.,Tang, S.,Ge, X.,Ju, B.,Yan, R.,Zhang, Z.
Structure and function of a pair of non-competing monoclonal antibodies against Langya henipavirus attachment glycoprotein.
Cell Rep, 44:116407-116407, 2025

PubMed Abstract: 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.

PubMed: 41071677
DOI: 10.1016/j.celrep.2025.116407

Experimental method

ELECTRON MICROSCOPY (2.92 Å)