期刊
JOURNAL OF VIROLOGY
卷 75, 期 5, 页码 2444-2451出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.75.5.2444-2451.2001
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资金
- NIAID NIH HHS [R01 AI015122, R37 AI011219, R01 AI039485, R01 AI032100, P01 AI045976, AI32100, R37 AI015122, AI39485, AI11219] Funding Source: Medline
Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses the same cellular receptor, 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 I; 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-1 binding 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.
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