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J Virol, July 1998, p. 5559-5564, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Epstein-Barr Virus (EBV) gN Homolog BLRF1 Encodes a 15-Kilodalton Glycoprotein That Cannot Be Authentically Processed unless It Is Coexpressed with the EBV gM Homolog BBRF3

Cathleen M. Lake, Sara J. Molesworth, and Lindsey M. Hutt-Fletcher*

School of Biological Sciences, University of Missouri---Kansas City, Kansas City, Missouri 64110

Received 25 February 1998/Accepted 3 April 1998

The Epstein-Barr virus (EBV) homolog of the conserved herpesvirus glycoprotein gN is predicted to be encoded by the BLRF1 open reading frame (ORF). Antipeptide antibody to a sequence corresponding to residues in the predicted BLRF1 ORF immunoprecipitated a doublet of approximately 8 kDa from cells expressing the BLRF1 ORF as a recombinant protein. In addition, four glycosylated proteins of 113, 84, 48, and 15 kDa could be immunoprecipitated from virus-producing cells by the same antibody. The 15-kDa species was the mature form of gN, which carried alpha 2,6-sialic acid residues. The remaining glycoproteins which associated with gN were products of the BBRF3 ORF of EBV, which encodes the EBV gM homolog. The 8-kDa doublet seen in cells expressing recombinant gN comprised precursors of the mature 15-kDa gN. Coexpression of EBV gM with EBV gN was required for authentic processing of the 8-kDa forms to the 15-kDa form.

* 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.

J Virol, July 1998, p. 5559-5564, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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