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Tern blot analysis (Fig. 2B and C). The purified complex contained two silver-stained bands of 110 and35 kDa (Fig. 2A, lane 3), although neither of these was prominent in the culture supernatant or column flowthrough (Fig. 2A, lanes 1 and 2). Both glycoproteins were readily detected in the culture supernatant by Western blot analysis (Fig. 2B and C, lanes 1). The absence of both gH and gL from th

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Staining (Fig. 2A, lane 3). LP11 reactivity is considered to be a critical test of gH-gL conformation, since this MAb reacts with gH only when it is part of the native complex (29). Second, LP11 neutralizes virus infectivity at high titers and therefore recognizes an immunologically important epitope (4). Purified gHt-gL was immuno-FIG. 2. Extracellular expression and purification of gHt-gL compl

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Ntrifugation at 30,000 g for 5 h through a 10 -30 -60 sucrose-PBS step gradient. The virus band located at the 30 -60 sucrose interface was collected, titered, and stored at 80 . Soluble HSV glycoproteins and infected cell extracts used. Soluble gD1(306t) was produced in baculovirus-infected Sf9 cells and was purified as previously described (52). Cytoplasmic extracts of HSV-1(NS) (16)- or HSV-