Coxsackievirus (CV) belongs to the Picornaviridae family and the Enterovirus genus. It is a non-enveloped, single-stranded, positive-sense RNA virus. The virus was first isolated and identified in 1948 from fecal samples of children in Coxsackie, New York, USA, and was named accordingly. Based on differences in pathogenicity in newborn mice, Coxsackievirus can be classified into group A (CV-A) and group B (CV-B). Group A includes 23 serotypes (CV-A1 to CV-A22, CV-A24), while group B includes 6 serotypes (CV-B1 to CV-B6). Different serotypes of Coxsackievirus exhibit diversity in genetic evolution, and the continuous variation of their genomes influences the virus's transmission capacity and antigenic properties.

Coxsackievirus particles exhibit a typical icosahedral symmetrical structure, with a diameter of approximately 28–30 nm. They lack a lipid envelope, making them highly resistant to heat, acids, and various disinfectants. The viral particles are formed by a protein capsid assembled from 60 copies of four structural proteins (VP1, VP2, VP3, and VP4), which encapsulate the viral genomic RNA. Among these, VP1, VP2, and VP3 proteins are exposed on the surface of the viral particles and together constitute the outer shell of the capsid, determining the virus's antigenicity and receptor-binding specificity. The VP4 protein is located inside the capsid, interacts with the genomic RNA, and plays a critical role in maintaining capsid stability and the viral uncoating process. A depression called the "canyon" exists on the viral surface and serves as a key binding site for cellular receptors (such as CAR and DAF). The Coxsackievirus genome is a single-stranded, positive-sense RNA, approximately 7.4 kb in length, containing a single open reading frame that encodes a polyprotein precursor. This precursor is processed by virus-encoded proteases to ultimately produce 11 mature proteins, including 4 structural proteins and 7 nonstructural proteins. The nonstructural proteins are primarily involved in viral genome replication, polyprotein processing, and the regulation of host cell physiological functions. High-resolution structural analysis of Coxsackievirus capsid proteins, particularly VP1, provides important molecular insights into its receptor recognition mechanisms and antigenic epitope distribution.

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