Efficient purification of Epstein-Barr virus membrane antigen gp340 by fast protein liquid chromatography

A rapid and efficient procedure for the isolation of Epstein-Barr (EB) virus membrane glycoprotein gp340 has been developed. The mild, two step method consisted of anion exchange chromatography of B95-8 cell membrane detergent extracts followed by further purification by gel filtration. Production of homogeneous gp340 was achieved routinely with recoveries of at least 35% from starting material. The purified molecule, when injected into mice with a synthetic muramyl dipeptide adjuvant, N-acetylmuramyl-L-threonyl-D-isoglutamine ((Thr1)MDP), elicited high titres of EB virus-neutralizing antibody.