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- Title
The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus.
- Authors
Guo, Yingying; Wu, Songyue; Li, Wenting; Yang, Haonan; Shi, Tianhao; Ju, Bin; Zhang, Zheng; Yan, Renhong
- 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 membrane fusion process. Our findings enhance the understanding of emerging HNVs that cause human diseases through zoonotic transmission and provide implication for LayV related vaccine development. In this work, the authors report the full-length structure of the attachment glycoprotein from Langya Henipavirus, which could enhance the understanding of emerging Henipavirus and provide important clues for vaccine development in the future.
- Subjects
CHINA; HENIPAVIRUSES; EPHRIN receptors; ZOONOSES; MEMBRANE fusion; EMERGING infectious diseases; VACCINE development
- Publication
Nature Communications, 2024, Vol 15, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-024-45202-5