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  • Newcombe, Nicole GUniversity of Newcastle (author)

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

  • Article/chapterEnglish2003

Publisher, publication year, extent ...

  • London :Society for General Microbiology,2003
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:hik-942
  • https://urn.kb.se/resolve?urn=urn:nbn:se:hik:diva-942URI
  • https://doi.org/10.1099/vir.0.19329-0DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

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  • Andersson, PerHögskolan i Kalmar,Naturvetenskapliga institutionen (author)
  • Johansson, E SusanneUniversity of Newcastle (author)
  • Au, Gough GUniversity of Newcastle (author)
  • Lindberg, A. MichaelHögskolan i Kalmar,Naturvetenskapliga institutionen(Swepub:lnu)nlimi (author)
  • Barry, Richard DUniversity of Newcastle (author)
  • Shafren, Darren RUniversity of Newcastle (author)
  • University of NewcastleNaturvetenskapliga institutionen (creator_code:org_t)

Related titles

  • In:Journal of General VirologyLondon : Society for General Microbiology84:Pt 11, s. 3041-30500022-13171465-2099

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