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Cellular receptor interactions of C-cluster human group A coxsackieviruses.

Newcombe, Nicole G (author)
University of Newcastle
Andersson, Per (author)
Högskolan i Kalmar,Naturvetenskapliga institutionen
Johansson, E Susanne (author)
University of Newcastle
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Au, Gough G (author)
University of Newcastle
Lindberg, A. Michael (author)
Högskolan i Kalmar,Naturvetenskapliga institutionen
Barry, Richard D (author)
University of Newcastle
Shafren, Darren R (author)
University of Newcastle
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 (creator_code:org_t)
London : Society for General Microbiology, 2003
2003
English.
In: Journal of General Virology. - London : Society for General Microbiology. - 0022-1317 .- 1465-2099. ; 84:Pt 11, s. 3041-3050
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Keyword

Virology
Virologi
Virologi
Virology

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