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J Gen Virol 71 (1990), 873-880; DOI 10.1099/0022-1317-71-4-873
© 1990 Society for General Microbiology

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Structural and immunological characterization of human cytomegalovirus gp55-116 (gB) expressed in insect cells

David E. Wells1, Leone G. Vugler2 and William J. Britt1,2,

1 Department of Microbiology
and2 Department of Pediatrics, University of Alabama at Birmingham, School of Medicine, Birmingham, Alabama 35294

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 Mr 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.

Received 21 August 1989; accepted 20 November 1989.





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