Dengue virus belongs to the Flaviviridae family, genus Flavivirus, and is an enveloped, single-stranded, positive-sense RNA virus. Primarily transmitted by vector insects such as Aedes aegypti and Aedes albopictus, it is one of the most widely distributed and rapidly spreading mosquito-borne viruses globally, posing a significant public health challenge in tropical and subtropical regions. Dengue virus exists in four distinct serotypes (DENV-1 to DENV-4), which can induce cross-reactive immune responses but lack long-lasting cross-protective immunity. Infection in humans can elicit antibodies that are cross-reactive but exhibit uneven neutralizing capabilities, a key scientific issue in dengue virus research. The virus maintains a "human-mosquito-human" transmission cycle in nature, and its global distribution is closely linked to the ecological range of vector mosquitoes and climate change.

The dengue virion is spherical, approximately 50 nm in diameter, and exhibits typical flavivirus structural features. From the inside out, the virion consists of three main components: the innermost is the nucleocapsid, formed by the viral genomic RNA bound to the capsid protein C; the middle layer is a lipid bilayer envelope derived from the host cell's endoplasmic reticulum membrane, embedded with viral membrane protein M and envelope protein E; the outermost layer is a regular surface structure formed by 180 copies of E and M proteins arranged as dimers. The E protein is the major surface protein of the virus, responsible for receptor binding and membrane fusion. It comprises three distinct structural domains, with domain III containing the primary type-specific and neutralizing antigenic epitopes. The viral genome is approximately 11 kb in length and encodes three structural proteins and seven non-structural proteins. The non-structural protein NS1 plays a crucial role in viral replication and immune regulation, NS3 possesses protease and helicase activities, and NS5 functions as an RNA-dependent RNA polymerase. On the surface of mature virions, the E proteins are arranged head-to-tail as dimers, forming a relatively smooth surface—a unique structural feature closely related to the virus's infectivity and antigenicity.

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