Fig. 1 HRV genomic structure (Jacobs SE, et al. 2013)
Fig. 2 Viral replication in airway epithelial cells (Jacobs SE, et al. 2013)
Rhinovirus, member of the genus Enterovirus family Picornaviridae, is a positive-sense, single-stranded-RNA (ssRNA) virus of approximately 7.2 kb. Currently, more than 160 sero-/genotypes have been described and classified into three species, RV-A, RV-B and RV-C. Sequencing and serologic methods have defined approximately 83 HRV-A types, 32 HRV-B types, and 55 HRV-C types with potentially as many as 150 to 170 serological distinct HRV types in circulation. Human rhinoviruses (HRVs) were first discovered in the 1950s in an effort to identify the etiology of the common cold. While once thought to cause relatively benign upper respiratory tract illness, HRVs also are important cause of otitis media and sinusitis and can precipitate exacerbations of asthma in children. Rhinovirus infection may play role in other illnesses that result in hospitalization of young children. Transmission of HRVs occurs primarily between individuals by either direct contact, contact with fomites, or aerosols.
HRV is a non-enveloped virus with a positive-sense single-stranded RNA that encodes 11 proteins. The viral polyprotein is divided into a P1 region, which encodes the capsid proteins VP1, VP2, VP3, and VP4, and the P2 and P3 regions, which include proteins 2APro, 2B, 2C, 3A, 3B (VPg), 3CPro, and 3DPol. Four proteins, VP1, VP2, VP3, and VP4, make up the viral capsid that encases the RNA genome, while the remaining nonstructural proteins are involved in viral replication and subsequent assembly. Antigenic variation among HRV types is derived from variations in the exposed surface of VP1, VP2, and VP3, while embedded VP4 is responsible for RNA packaging during assembly. Compared to the rest of the HRV genome, the capsid proteins exhibit a high degree of heterogeneity resulting in a wide range of antigenic diversity. There are 60 copies each of the four capsid proteins, giving the virion an icosahedral structure, with a canyon in VP1 that serves as the site of attachment to cell surface receptors.
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