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J Gen Virol 71 (1990), 2107-2114; DOI 10.1099/0022-1317-71-9-2107
© 1990 Society for General Microbiology

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The antigenic structure of dengue type 1 virus envelope and NS1 proteins expressed in Escherichia coli

Peter W. Mason1, Martin U. Zügel2, Anthony R. Semproni2, Maurille J. Fournier2 and Thomas L. Mason2

1 Yale Arbovirus Research Unit, Yale University School of Medicine, New Haven, Connecticut 06510
and2 Department of Biochemistry and Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003, U.S.A.

The antigenic structures of the envelope protein, E, and the non-structural protein, NS1, of dengue type 1 virus (DEN1) have been studied in the form of recombinant fusion proteins expressed in Escherichia coli. Deletion analysis was used to identify two distinct antigenic domains in E that reacted with subsets of antiviral monoclonal antibodies (MAbs). Domain I of E extends from amino acid residues (aa) 76 to 93 of E; domain II extends from aa 293 to 402 and contains an essential disulphide bridge. MAbs also reacted with several determinants clustered near the N terminus of the NS1 protein (aa 57 to 126). Recombinant fusion proteins containing E. coli trpE sequences and most of the sequences for either E or NS1 were immunogenic in mice. The antibodies elicited by the E fusion protein reacted with a portion of the protein containing domain II, whereas antibodies elicited by the NS1 fusion protein did not react with the antigenic determinants defined by our MAbs.

Received 26 January 1990; accepted 15 May 1990.


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