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J Gen Virol 70 (1989), 2843-2851; DOI 10.1099/0022-1317-70-11-2843
© 1989 Society for General Microbiology

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The Cloning and Expression in Escherichia coli of Sequences Coding for p24, the Core Protein of Human Immunodeficiency Virus, and the Use of the Recombinant Protein in Characterizing a Panel of Monoclonal Antibodies against the Viral p24 Protein

R. P. Spence1, W. M. Jarvill2, R. B. Ferns3, R. S. Tedder3 and D. Parker2

1 Department of Molecular Biology, Wellcome Biotech
and2 Wellcome Diagnostics R & D, Langley Court, Beckenham, Kent BR3 3BS
and3 Virology Section, Department of Medical Microbiology, Middlesex Hospital Medical School, Riding House Street, London W1P 7PN, U.K.

The sequences encoding the p24 core protein of human immunodeficiency virus type 1 were identified in a cDNA library made from infected CEM cells. The nucleotide sequence of the DNA coding for p24 was shown to be very similar but not identical to the sequences of lymphadenopathy virus and human T-cell leukaemia virus type IIIb. These sequences were expressed in Escherichia coli at the amino terminus of beta-galactosidase and used to screen a panel of monoclonal antibodies raised against virus-expressed p24. Regions containing the epitopes of five of the monoclonal antibodies were located using a series of amino- and carboxy-terminal deletion mutants of the recombinant p24 protein.

Keywords: HIV, monoclonal antibodies, recombinant proteins

Received 17 October 1988; accepted 29 June 1989.





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Copyright © 1989 by the Society for General Microbiology.