Structures of phlebovirus glycoprotein Gn and identification of a neutralizing antibody epitope

Authors: Yan Wu, Yaohua Zhu, Feng Gao, Yongjun Jiao, Babayemi Olawale Oladejo, Yan Chai, Yuhai Bi, Shan Lu, Meng‐Qiu Dong, Chang Zhang, Guangmei Huang, Gary Wong, Na Li, Yanfang Zhang, Yan Li, Wenhai Feng, Yi Shi, Mifang Liang, Rongguang Zhang, Jianxun Qi, George F. Gao - Proceedings of the National Academy of Sciences, PNAS 2017 cited by 164

Significance Bunyaviruses are emerging zoonotic pathogens of public-health concern. Lack of structures for proteins on the viral membrane (“envelope”) surface limits understanding of entry. We describe atomic-level structures for the globular “head” of the envelope protein, glycoprotein N (Gn), from two members, severe fever with thrombocytopenia syndrome virus (SFTSV) and Rift Valley fever virus (RVFV), of Phleboviruses genus in the bunyavirus family, and a structure of the SFTSV Gn bound with a neutralizing antibody Fab. The results show the folded Gn structure and define virus-specific neutralizing-antibody binding sites. Biochemical assays suggest that dimerization, mediated by conserved cysteines in the region (“stem”) connecting the Gn head with the transmembrane domain, is a general feature of bunyavirus envelope proteins and that the dimer is probably the olimeric form on the viral surface.