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Journal of Virology, September 1998, p. 7577-7582, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Epstein-Barr Virus Recombinant Lacking Expression
of Glycoprotein gp150 Infects B Cells Normally but Is Enhanced for
Infection of Epithelial Cells
Corina M.
Borza and
Lindsey M.
Hutt-Fletcher*
School of Biological Sciences, University of
Missouri
Kansas City, Kansas City, Missouri 64110
Received 5 March 1998/Accepted 20 May 1998
Glycoprotein gp150 is a highly glycosylated protein encoded by the
BDLF3 open reading frame of Epstein-Barr virus (EBV). It does not have
a homolog in the alpha- and betaherpesviruses, and its function is not
known. To determine whether the protein is essential for replication of
EBV in vitro, a recombinant virus which lacked its expression was made.
The recombinant virus had no defects in assembly, egress, binding, or
infectivity for B cells or epithelial cells. Infection of epithelial
cells was, however, enhanced. The glycoprotein was sensitive to
digestion with a glycoprotease that digests sialomucins, but no
adhesion to cells that express selectins that bind to sialomucin
ligands could be detected.
*
Corresponding author. Mailing address: School of
Biological Sciences, University of Missouri
Kansas City, 5007 Rockhill
Rd., Kansas City, MO 64110. Phone: (816) 235-2575. Fax: (816) 235-5595. E-mail: huttfletcher{at}cctr.umkc.edu.
Journal of Virology, September 1998, p. 7577-7582, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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