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.

The Journal of General Virology
R P SpenceP E Highfield

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 beta-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.

Citations

Sep 1, 1990·AIDS Research and Human Retroviruses·J D OramJ W Carswell
Oct 1, 1990·AIDS Research and Human Retroviruses·L S EhrlichC A Carter
Jan 31, 1991·Nature·R A Weiss
Nov 18, 2014·World Journal of Gastroenterology : WJG·Emanuele SinagraAroldo Gabriele Rizzo
Jan 1, 1992·Archives of Virology·T FuruyaT Mikami

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