Classical Swine Fever Virus (CSFV) belongs to the Flaviviridae family and the Pestivirus genus. It is an enveloped, single-stranded positive-sense RNA virus. This virus is the causative agent of classical swine fever, and since its first official report in Ohio, USA, in 1833, it has become one of the most devastating diseases in the global swine industry. The global distribution of the virus exhibits regional characteristics. While it has been eradicated through strict control measures in some countries (such as EU member states and North America), it remains endemic in regions like Asia, Africa, and South America. Based on genomic sequence differences, Classical Swine Fever Virus can be classified into three genotypes and multiple subtypes, with variations in virulence, antigenicity, and geographical distribution among them. The virus exhibits strong environmental resistance and can remain infectious for extended periods under suitable conditions.

The Classical Swine Fever Virus particle is spherical, with a diameter of approximately 40–60 nm, exhibiting typical pestivirus structural features. The outermost layer of the virion is an envelope composed of a viral lipid bilayer, uniformly embedded with virus-encoded glycoproteins E2 and Erns. Among these, the E2 protein forms surface spikes as homodimers and is the key protein for virus binding to host cell receptors and inducing neutralizing antibodies. The Erns protein, on the other hand, possesses ribonuclease activity and plays a role in viral immune evasion. Inside the envelope lies a core structure formed by the capsid protein C tightly bound to the viral genomic RNA. The Classical Swine Fever Virus genome is a single-stranded positive-sense RNA, approximately 12.3 kb in length, containing only one open reading frame that encodes a polyprotein precursor. This precursor is processed by host and viral proteases into at least 12 mature proteins, including 4 structural proteins and 8 nonstructural proteins. Among these, the NS5B protein possesses RNA-dependent RNA polymerase activity and is responsible for viral genome replication. The virus assembles within the host cell's endoplasmic reticulum and is released via the cellular secretory pathway. The antigenic structure of the viral surface E2 protein is complex, containing multiple important conformational-dependent and linear epitopes, which form the primary molecular basis for distinguishing different strains and vaccine development.

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