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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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