8WJB

Structural insights into the Langya virus attachment glycoprotein

Summary for 8WJB

• Entry DOI: 10.2210/pdb8wjb/pdb
• Descriptor: Attachment glycoprotein (1 entity in total)
• Functional Keywords: attachment glycoprotein, viral protein
• Biological source: Henipavirus
• Total number of polymer chains: 2
• Total formula weight: 94025.98

Authors

Jun, L.,Chenghai, W. (deposition date: 2023-09-25, release date: 2024-10-02, Last modification date: 2025-04-16)

Primary citation

Wang, C.,Li, M.,Wang, Y.,Ding, Q.,Fan, S.,Lan, J.
Structural insights into the Langya virus attachment glycoprotein.
Structure, 32:1090-1098.e3, 2024

PubMed Abstract: Langya virus (LayV) was recently detected in patients with acute pneumonic diseases in China. Genome alignment indicated that LayV is a type of zoonotic henipavirus (HNV) that might also infect domestic animals. Previous studies revealed that HNVs mainly use ephrin-B1, ephrin-B2, or ephrin-B3 as cell receptors and the attachment glycoprotein (G) is the host cell receptor-binding protein. However, the LayV receptor remains unknown. Here, we present the 2.77 Å crystal structure of the LayV G C-terminal domain (CTD). We show that the LayV G protein CTD possesses a similar architecture as the Mojiang virus (MojV) G protein but is markedly different from the Nipah virus (NiV), Hendra virus (HeV), and Cedar virus (CedV) G proteins. Surface plasmon resonance (SPR) experiments indicate that LayV G does not bind ephrin-B proteins. Steric hindrance may prevent interactions between LayV G and ephrin-B. Our data might facilitate drug development targeting LayV.

PubMed: 38815575
DOI: 10.1016/j.str.2024.05.003

Experimental method

X-RAY DIFFRACTION (2.75 Å)