Virus Name | coxsackievirus A21 |
Virus Short Name | CV-A21 |
Order | Picornavirales |
Virus Family | Picornaviridae |
Virus Subfamily | N.A. |
Genus | Enterovirus |
Species | Enterovirus C |
Host | Human, mammals |
Cell Tropism | Upper respiratory tract |
Associated Disease | Respiratory disease |
Mode of Transmission | Feces,saliva, nasal mucus, or sputum |
VIPR DB link | https://www.viprbrc.org/brc/home.spg?decorator=picorna |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/234/picornaviridae |
Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Picornaviridae |
Paper Title | Interaction of coxsackievirus A21 with its cellular receptor, ICAM-1 |
Author's Name | Xiao C, Bator CM, Bowman VD, Rieder E, He Y, Hebert B, Bella J, Baker TS, Wimmer E, Kuhn RJ, Rossmann MG. |
Journal Name | Journal Of Virology |
Pubmed ID | 11160747 |
Abstract | Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses the same cellularreceptor, intercellular adhesion molecule 1 (ICAM-1), as does the major group of HRVs unlike HRVs, however, it is stable at acid pH. The cryoelectron microscopy (cryoEM) image reconstruction of CAV21 is consistent with the highly homologous crystal structure of poliovirus 1 like other enteroviruses and HRVs, CAV21 has a canyon-like depression around each of the 12 fivefold vertices. A cryoEM reconstruction of CAV21 complexed with ICAM-1 shows all five domains of the extracellular component of ICAM-1. The known atomic structure of the ICAM-1 amino-terminal domains D1 and D2 has been fitted into the cryoEM density of the complex. The site of ICAM-1binding within the canyon of CAV21 overlaps the site of receptor recognition utilized by rhinoviruses and polioviruses. Interactions within this common region may be essential for triggering viral destabilization after attachment to susceptible cells. |
Used Model | HeLa cells |
DOI | 10.1128/JVI.75.5.2444-2451.2001 |