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The Severe fever with thrombocytopenia syndrome virus (SFTSV) glycoprotein Gn is a critical structural component of the viral envelope, primarily responsible for host cell attachment and entry (Wu et al., 2017, PMID: 28978461). SFTSV, a member of the Bandavirus genus (recently reclassified as Dabie bandavirus), causes a severe tick-borne illness characterized by high fever, thrombocytopenia, and multi-organ failure, with mortality rates ranging from 12% to 30% (Yu et al., 2011, PMID: 21410387). The Gn protein forms heterodimers with the Gc protein on the virion surface, where the Gn ectodomain serves as the primary target for the host's neutralizing antibody response (Kim et al., 2019, PMID: 30700611). Research indicates that the Gn ectodomain contains the receptor-binding domain (RBD) that interacts with host factors like DC-SIGN and L-SIGN to facilitate viral internalization via endocytosis (Hofmann et al., 2013, PMID: 23760237). Because of its accessibility on the viral surface and its essential role in the infection cycle, the Gn ectodomain is a focal point for the development of vaccines and therapeutic monoclonal antibodies, such as MAb 4-5 and Sabin-1, which aim to neutralize the virus by blocking its ability to infect susceptible host cells.
Neutralization of viral infectivity by binding to the Gn ectodomain, which sterically hinders the interaction between the virus and host cell receptors (such as DC-SIGN) and inhibits subsequent viral entry and membrane fusion.
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