Conserved Receptor-Binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Shared Receptor
Abstract
The GP(sub 1,2) envelope glycoproteins 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 GP(sub 1) subunit bound filovirus-permissive cell lines more efficiently than full-length GP (sub 1). A homologous 148-amino acid fragment of the Zaire ebolavirus GP(sub 1) subunit similarly bound the same cell lines more efficiently than a series of longer GP(sub 1)-truncation variants. Neither the marburgvirus GP(SUB 1) fragment, nor that of ebolavirus, bound a non-permissive 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(sub 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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 14, 2006
- Accession Number
- ADA449224
Entities
People
- Alexander C. Guth
- Hyeryun Choe
- Jens H. Kuhn
- Jonathan S Towner
- Kelly Lyn Warfield
- Martin J. Vincent
- Sheli R. Radoshitzky
- Sina Bavari
- Stuart T. Nichol
- Wenhui Li
Organizations
- United States Army Medical Research Institute of Infectious Diseases