Nat Commun. 2024 Jan 27;15(1):812.
Affiliations
- Department of Biochemistry, School of Medicine, Key University Laboratory of Metabolism and Health of Guangdong, Institute for Biological Electron Microscopy, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, China. guoyingnba@163.com.
- Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen, China.
- The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Shenzhen, China.
- Department of Biochemistry, School of Medicine, Key University Laboratory of Metabolism and Health of Guangdong, Institute for Biological Electron Microscopy, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, China.
- Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen, China. jubin2013@163.com.
- The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Shenzhen, China. jubin2013@163.com.
- Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen, China. zhangzheng1975@aliyun.com.
- The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Shenzhen, China. zhangzheng1975@aliyun.com.
- Department of Biochemistry, School of Medicine, Key University Laboratory of Metabolism and Health of Guangdong, Institute for Biological Electron Microscopy, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, China. yanrh@sustech.edu.cn.
PMID: 38280880 DOI: 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 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.
References
- Eaton BT, Broder CC, Middleton D, Wang LF. Hendra and Nipah viruses: different and dangerous. Nat. Rev. Microbiol. 2006;4:23–35. doi: 10.1038/nrmicro1323.
- Field H, et al. The natural history of Hendra and Nipah viruses. Microbes. Infect. 2001;3:307–314. doi: 10.1016/S1286-4579(01)01384-3.
- Weatherman S, Feldmann H, de Wit E. Transmission of henipaviruses. Curr. Opin. Virol. 2018;28:7–11. doi: 10.1016/j.coviro.2017.09.004.
- Madera S, et al. Discovery and Genomic Characterization of a Novel Henipavirus, Angavokely Virus, from Fruit Bats in Madagascar. J. Virol. 2022;96:e0092122. doi: 10.1128/jvi.00921-22.
- Zhang XA, et al. A Zoonotic Henipavirus in Febrile Patients in China. N. Engl J. Med. 2022;387:470–472. doi: 10.1056/NEJMc2202705.
