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Journal of Virology, February 2004, p. 1431-1439, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1431-1439.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Enterovirus Capsid Interactions with Decay-Accelerating Factor Mediate Lytic Cell Infection

Nicole G. Newcombe,1 E. Susanne Johansson,1 Gough Au,1 A. Michael Lindberg,2 Richard D. Barry,1 and Darren R. Shafren1*

The Picornaviral Research Unit, School of Biomedical Sciences, Faculty of Health, The University of Newcastle, Newcastle, New South Wales 2300, Australia,1 Department of Chemistry and Biomedical Sciences, University of Kalmar, SE-391 82 Kalmar, Sweden2

Received 24 July 2003/ Accepted 10 October 2003

The cellular receptor usage of numerous human enteroviruses can differ significantly between low-cell-culture-passaged clinical isolates and highly laboratory-passaged prototype strains. The prototype strain of coxsackievirus A21 (CVA21) displays a dual-receptor specificity as determined with a receptor complex consisting of decay-accelerating factor (DAF) and intercellular adhesion molecule 1 (ICAM-1). In this study, the cellular receptor interactions of low-cell-passage CVA21 clinical isolates with respect to their interactions with cell surface-expressed DAF and ICAM-1 were compared to those of the CVA21 prototype (Kuykendall) strain. Dual-receptor usage of DAF and ICAM-1 by CVA21 clinical isolates was confirmed by cell transfection and radiolabeled binding assays. The cellular attachment of clinical and prototype CVA21 strains to cells that coexpressed DAF and ICAM-1 was not additive compared to the viral binding to cells expressing one or other receptor. In fact, the binding data suggest there is an inhibition of CVA21 cellular attachment in environments where high-level coexpression of both DAF and ICAM-1 occurs. Antibody cross-linking of DAF rendered cells susceptible to lytic infection by the CVA21 clinical isolates. In a novel finding, three clinical isolates could, to various degrees, infect and lyse DAF-expressing cells in the absence of DAF-antibody cross-linking and ICAM-1 expression. Sequence analysis of the P1 region of clinical and prototype virus genomes identified a number of coding changes that may contribute to the observed enhanced DAF usage phenotype of the clinical CVA21 isolates. None of the amino acid changes was located in the previously postulated ICAM-1 footprint, a receptor-binding environment that was conserved on the capsid surface of all CVA21 clinical isolates. Taken together, the data suggest that community-circulating strains of CVA21 can infect target cells expressing either ICAM-1 or DAF alone and that such interactions extend tissue tropism and impact directly on viral pathogenesis.

* Corresponding author. Mailing address: The Picornaviral Research Unit, School of Biomedical Sciences, Faculty of Health, The University of Newcastle, Level 3, David Maddison Clinical Sciences Building, Royal Newcastle Hospital, Newcastle, 2300, New South Wales, Australia. Phone: 61-2-4923-6158. Fax: 61-2-4923-6814. E-mail: dshafren{at}mail.newcastle.edu.au.

Journal of Virology, February 2004, p. 1431-1439, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1431-1439.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Milstone, A. M., Petrella, J., Sanchez, M. D., Mahmud, M., Whitbeck, J. C., Bergelson, J. M. (2005). Interaction with Coxsackievirus and Adenovirus Receptor, but Not with Decay-Accelerating Factor (DAF), Induces A-Particle Formation in a DAF-Binding Coxsackievirus B3 Isolate. J. Virol. 79: 655-660 [Abstract] [Full Text]  
  • Johansson, E. S., Xing, L., Cheng, R. H., Shafren, D. R. (2004). Enhanced Cellular Receptor Usage by a Bioselected Variant of Coxsackievirus A21. J. Virol. 78: 12603-12612 [Abstract] [Full Text]  
  • Newcombe, N. G., Beagley, L. G., Christiansen, D., Loveland, B. E., Johansson, E. S., Beagley, K. W., Barry, R. D., Shafren, D. R. (2004). Novel Role for Decay-Accelerating Factor in Coxsackievirus A21-Mediated Cell Infectivity. J. Virol. 78: 12677-12682 [Abstract] [Full Text]  


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