Epstein-Barr virus recombinant lacking expression of glycoprotein gp150 infects B cells normally but is enhanced for infection of epithelial cells.

Borza CM, Hutt-Fletcher LM
J Virol. 1998 72 (9): 7577-82

PMID: 9696856 · PMCID: PMC110006 · DOI:10.1128/JVI.72.9.7577-7582.1998

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.

MeSH Terms (13)

B-Lymphocytes Cell Line E-Selectin Epithelial Cells Glycoproteins Herpesvirus 4, Human Humans Metalloendopeptidases Open Reading Frames P-Selectin Plasmids Recombination, Genetic Viral Proteins

Connections (1)

This publication is referenced by other Labnodes entities: