Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor.
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.
Kuhn
Jens H
JH
Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, Massachusetts 01772, USA.
Radoshitzky
Sheli R
SR
Guth
Alexander C
AC
Warfield
Kelly L
KL
Li
Wenhui
W
Vincent
Martin J
MJ
Towner
Jonathan S
JS
Nichol
Stuart T
ST
Bavari
Sina
S
Choe
Hyeryun
H
Aman
M Javad
MJ
Farzan
Michael
M
D000595:Amino Acid Sequence; D000818:Animals; D002522:Chlorocebus aethiops; D029043:Ebolavirus / Q000378:metabolism*; D006801:Humans; D019169:Jurkat Cells; D029024:Marburgvirus / Q000378:metabolism*; D008969:Molecular Sequence Data; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014709:Vero Cells
D011991:Receptors, Virus