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Journal of Virology, August 2001, p. 7078-7085, Vol. 75, No. 15
Department of Neuropharmacology, Division of
Virology, The Scripps Research Institute, La Jolla, California
92037,1 and Department of Molecular
Sciences, University of Tennessee Health Science Center, Memphis,
Tennessee 381632
Received 22 January 2001/Accepted 30 April 2001
Borna disease virus (BDV) surface glycoprotein (GP) (p56) has a
predicted molecular mass of 56 kDa. Due to extensive posttranslational glycosylation the protein migrates as a polypeptide of 84 kDa (gp84).
The processing of gp84 by the cellular protease furin generates gp43,
which corresponds to the C-terminal part of gp84. Both gp84 and gp43
have been implicated in viral entry involving receptor-mediated
endocytosis and pH-dependent fusion. We have investigated the domains
of BDV p56 involved in virus entry. For this, we used a pseudotype
approach based on a recently developed recombinant vesicular stomatitis
virus (VSV) in which the gene for green fluorescent protein was
substituted for the VSV G protein gene (VSV
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.15.7078-7085.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
N-Terminal Domain of Borna Disease Virus G (p56)
Protein Is Sufficient for Virus Receptor Recognition and Cell
Entry


G*). Complementation of
VSV
G* with BDV p56 resulted in infectious VSV
G* pseudotypes that
contained both BDV gp84 and gp43. BDV-VSV chimeric GPs that
contained the N-terminal 244 amino acids of BDV p56 and amino acids 421 to 511 of VSV G protein were efficiently incorporated into VSV
G*
particles, and the resulting pseudotype virions were neutralized by
BDV-specific antiserum. These findings indicate that the N-terminal
part of BDV p56 is sufficient for receptor recognition and virus entry.
*
Corresponding author. Mailing address: The Scripps
Research Institute, IMM6, 10550 N. Torrey Pines Rd., La Jolla, CA
92037. Phone: (858) 784-9462. Fax: (858) 784-9981. E-mail:
juanct{at}scripps.edu.
Publication 13774-NP from The Scripps Research Institute.
Present address: Department of Microbiology, Akita University
School of Medicine, Akita, Japan.
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