PMID: 38280880 PMCID: PMC10821904 DOI: 10.1038/s41467-024-45202-5
Abstract
Langya Henipavirus (LayV) infection is an emerging zoonotic disease that has been causing respiratory symptoms in China since 2019. For virus entry, LayV's genome encodes the fusion protein F and the attachment glycoprotein G. However, the structural and functional information regarding LayV-G remains unclear. In this study, we revealed that LayV-G cannot bind to the receptors found in other HNVs, such as ephrin B2/B3, and it shows different antigenicity from HeV-G and NiV-G. Furthermore, we determined the near full-length structure of LayV-G, which displays a distinct mushroom-shaped configuration, distinguishing it from other attachment glycoproteins of HNV. The stalk and transmembrane regions resemble the stem and root of mushroom, and four downward-tilted head domains as mushroom cap potentially interact with the F protein and influence the membrane fusion process. Our findings enhance the understanding of emerging HNVs that cause human diseases through zoonotic transmission and provide implications for LayV-related vaccine development.
Keywords: Langya Henipavirus; LayV; attachment glycoprotein G; zoonotic transmission; vaccine development.
