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Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor

Academic Article
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Overview

authors

  • Kuhn, J. H.
  • Radoshitzky, S. R.
  • Guth, A. C.
  • Warfield, K. L.
  • Li, W. H.
  • Vincent, M. J.
  • Towner, J. S.
  • Nichol, S. T.
  • Bavari, S.
  • Choe, Hyeryun
  • Aman, M. J.
  • Farzan, Michael

publication date

  • June 2006

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The GP(1,2) envelope glycoproteins (GP) of filoviruses (marburg- and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells. Here we show that a 151-amino acid fragment of the Lake Victoria marburgvirus GP1 subunit bound filovirus-permissive cell lines more efficiently than full-length GP1. An homologous 148-amino acid fragment of the Zaire ebolavirus GP1 subunit similarly bound the same cell lines more efficiently than a series of longer GP1 truncation variants. Neither the marburgvirus GP1 fragment nor that of ebolavirus bound a nonpermissive lymphocyte cell line. Both fragments specifically inhibited replication of infectious Zaire ebolavirus, as well as entry of retroviruses pseudotyped with either Lake Victoria marburgvirus or Zaire ebolavirus GP(1,2). These studies identify the receptor-binding domains of both viruses, indicate that these viruses utilize a common receptor, and suggest that a single small molecule or vaccine can be developed to inhibit infection of all filoviruses.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cercopithecus aethiops
  • Ebolavirus
  • Humans
  • Jurkat Cells
  • Marburgvirus
  • Molecular Sequence Data
  • Receptors, Virus
  • Sequence Homology, Amino Acid
  • Vero Cells
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M601796200

PubMed ID

  • 16595665
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Additional Document Info

start page

  • 15951

end page

  • 15958

volume

  • 281

issue

  • 23

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