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J Gen Virol 74 (1993), 491-494; DOI 10.1099/0022-1317-74-3-491
© 1993 Society for General Microbiology

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Induction of neutralizing antibodies by varicella-zoster virus gpII glycoprotein expressed from recombinant vaccinia virus

Marc Massaer, Michèle Haumont, Martine Place, Alex Bollen and Paul Jacobs

Service de Génétique Appliquée, Centre de Recherches Industrielles, Université Libre de Bruxelles, 24 rue de l'Industrie, B-1400 Nivelles, Belgium

The gpII glycoprotein of varicella-zoster virus (VZV) was produced in CV1 cells via vaccinia virus recombinants. Two different DNA constructs were expressed: the first one encodes the complete gpII protein (gpII s+a+) and the second a truncated species lacking the membrane anchorage domain (gpII s+a-). To achieve expression both coding sequences had to be engineered at the 5' end by substituting the unusually short (24 bp) natural signal sequence by a more conventional one encoding 29 amino acids. Recombinant gpII proteins were detected in vaccinia virus-infected cells by ELISA and immunoprecipitation. Both forms of recombinant gpII proteins were produced as glycosylated single-chain molecules of respectively 110K and 90K. Upon reduction these were only partially converted into subunits. A rabbit infected with the vaccinia virus recombinant expressing the complete gpII produced antibodies which recognized VZV antigens and neutralized VZV infectivity in vitro, independent of complement.

Received 7 July 1992; accepted 11 November 1992.


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L. Maresová, L. Kutinová, V. Ludvíková, R. Zák, M. Mares, and S. Nemecková
Characterization of interaction of gH and gL glycoproteins of varicella-zoster virus: their processing and trafficking
J. Gen. Virol., June 1, 2000; 81(6): 1545 - 1552.
[Abstract] [Full Text]




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Copyright © 1993 by the Society for General Microbiology.