Varicella-zoster virus (VZV) expresses six known glycoproteins. High level expression of recombinant soluble forms of the VZV glycoproteins E and I (gE and gI) was achieved in the baculovirus system. gE and gI associate in VZV-infected cells to form an intermolecular complex. To purify large amounts of these glycoproteins, gE was produced with a C-terminal six-histidine (HIS-6) tag sequence, and gI was produced both with and without the HIS-6 sequence. The individual glycoproteins or the gE/gI complex were purified in their native forms by use of affinity chromatography. Recombinant soluble VZV gE and gI provided important tools in the biochemical analysis and may contribute further to the functional and immunologic studies of these VZV envelope components.