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.
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 alpha2,6-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.
Lake
C M
CM
School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110, USA.
Molesworth
S J
SJ
Hutt-Fletcher
L M
LM
D005814:Genes, Viral; D006031:Glycosylation; D004854:Herpesvirus 4, Human / Q000235:genetics*; D008970:Molecular Weight; D016366:Open Reading Frames; D011994:Recombinant Proteins / Q000096:biosynthesis; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000378:metabolism
D011994:Recombinant Proteins; D014759:Viral Envelope Proteins