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The gene encoding the major envelope glycoprotein complex, gp55–116 (gB), of human cytomegalovirus (HCMV) was expressed at high levels in insect cells utilizing a recombinant baculovirus. The mature intracellular form of the insect-derived gp55–116 was a protein of M r 150K which contained approximately 50K of N-linked oligosaccharides. The oligosaccharide linkages were almost exclusively endoglycosidase H- sensitive. The 150K protein was processed, presumably by proteolytic cleavage, to yield at least one of the previously defined cleavage products of the gp55–116. This processing step was significantly less efficient in insect cells than the analogous step in mammalian cells. Finally, the insect-derived gp55–116 was highly immunogenic in experimental animals and readily recognized by antibodies contained within HCMV- immune human serum, suggesting that this recombinant protein warrants further study as a potential HCMV subunit vaccine candidate.
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