@article{mbs:/content/journal/jgv/10.1099/vir.0.19329-0, author = "Newcombe, Nicole G. and Andersson, Per and Johansson, E. Susanne and Au, Gough G. and Lindberg, A. Michael and Barry, Richard D. and Shafren, Darren R.", title = "Cellular receptor interactions of C-cluster human group A coxsackieviruses", journal= "Journal of General Virology", year = "2003", volume = "84", number = "11", pages = "3041-3050", doi = "https://doi.org/10.1099/vir.0.19329-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.19329-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The cellular receptor complex of coxsackievirus A21 (CVA21), a C-cluster human enterovirus, is formed by the subtle interaction of individual cellular receptors, decay accelerating factor (DAF) and intercellular adhesion molecule-1 (ICAM-1). In this receptor complex, DAF functions in the membrane sequestration of the virus, while the role of ICAM-1 is as the functional cellular internalization receptor. However, despite the elucidation of the CVA21–cell receptor interactions, there have been few definite investigations into cellular receptor usage of other coxsackie A viruses (CVAs) belonging to the C-cluster. In the present study, radiolabelled virus-binding assays demonstrated that CVA13, -15, -18 and -20, a subset of the human enterovirus C-cluster, bind directly to surface-expressed ICAM-1, but not to surface-expressed DAF. Furthermore, lytic infection of ICAM-1-expressing rhabdomyosarcoma (RD) cells by this C-cluster subset of viruses was inhibited by specific ICAM-1 monoclonal antibody blockade, except for that of CVA20. Despite possessing ICAM-1-binding capabilities, CVA20 employed an as yet unidentified internalization receptor for cell entry and subsequent productive lytic infection of ICAM-1-negative RD cells. In a further example of C-cluster cellular receptor heterogeneity, CVA13 exhibited significant binding to the surface of CHO cells expressing neither DAF nor ICAM-1. Despite a common receptor usage of ICAM-1 by this subset of C-cluster CVAs, the amino acid residues postulated to represent the ICAM-1-receptor footprint were not conserved.", }