Glycosylation pathways of two major Epstein-Barr virus membrane antigens

Abstract

Monoclonal antibodies to the Epstein-Barr virus (EBV) membrane antigens (MA) were used to delineate the sequence of events occurring during MA maturation. Immunoprecipitation experiments performed with B95-8 virus infected 1605L cells, pulse labeled in the presence of tunicamycin or 2-deoxyglucose, suggest that the nonglycosylated forms of the mature 236,000 (236K) and 86K MA have molecular weights of 149K and 69K, respectively. Monensin treatment results in the accumulation of a 189K antigen which is converted to the mature 236K MA after a 2 hr chase in the absence of monensin. Experiments with monensin also suggest that an 84K intermediate is involved in the formation of the mature 86K MA. The mature 236K MA is resistant to endoglycosidase H while the 189K intermediate and the mature 86K MA are partially sensitive to this enzyme. The mature 236K and 86K MA and the 189K intermediate are resistant to endoglycosidase D.