PURIFICATION AND CHARACTERIZATION OF RECOMBINANT VARICELLA-ZOSTER VIRUS GLYCOPROTEIN GPII, SECRETED BY CHINESE-HAMSTER OVARY CELLS

Chinese hamster ovary cells have been engineered to secrete an anchorl ess form of the varicella-zoster virus gpII protein. Purification of t he recombinant product was achieved by a combination of hydrophobic an d gel filtration chromatography giving rise to a protein more than 85% pure. Recombinant gpII was composed of several polypeptides which, on the basis of amino-terminal sequence analysis, corresponded to a 93-k Da precursor and to the N- and C-terminal subunits of the molecule (64 and 39/36 kDa, respectively). Ah polypeptides carried N-linked high-m annose and complex glycosylations, whereas O-glycosylations were carri ed by the precursor and the N-terminal subunits only. Surprisingly, pu rified recombinant gpII spontaneously formed large oligomeric structur es of variable size. These complexes contained noncovalently linked li pids. Mice inoculated with the recombinant gpII absorbed onto the weak adjuvant, aluminium hydroxide, produced virus neutralizing antibodies . The recombinant gpII may thus constitute a good candidate for the de velopment of a subunit vaccine against varicella-zoster virus. (C) 199 5 Academic Press, Inc.