The expression in Escherichia coli of sequences coding for the p18 protein of human immunodeficiency virus and the use of the recombinant protein in characterizing a panel of monoclonal antibodies against the viral p18 protein

R. P. Spence, J. Walker, W. M. Jarvill, R. B. Ferns, R. S. Tedder, Q. Sattentau, J. Weber, N. R. Parry, P. E. Highfield

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    Abstract

    The sequences coding for the p18 protein of CBL-1, a British human immunodeficiency virus (HIV) type 1 isolate, were expressed in Escherichia coli as β-galactosidase fusion proteins. The recombinant proteins were used to screen a panel of five monoclonal antibodies (MAbs) raised against p18 expressed in CBL-1-infected cells. The regions containing the epitopes for four of the MAbs were located using carboxy deletion mutants and synthetic peptides. The epitope of one of the MAbs (1D9) was reconstructed as part of an unfused, E. coli-expressed p18 protein using the polymerase chain reaction technique. Four different HIV strains and one lymphadenopathy virus type 2 strain were analysed by fluorescence-activated cell sorting of live infected cells using the p18-reactive MAbs.

    Original languageEnglish
    Pages (from-to)2853-2863
    Number of pages11
    JournalJournal of General Virology
    Volume70
    Issue number11
    DOIs
    Publication statusPublished - 1989

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    Copyright 2017 Elsevier B.V., All rights reserved.

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