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High‐level expression and epitope localization of the major outer membrane protein of Chlamydia trachomatis serovar L1
Author(s) -
Pickett M. A.,
Ward M. E.,
Clarke I. N.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00077.x
Subject(s) - biology , porin , epitope , bacterial outer membrane , chlamydia trachomatis , recombinant dna , monoclonal antibody , serotype , escherichia coli , microbiology and biotechnology , plasmid , lac operon , virology , gene , antibody , genetics
Summary Fragments of the gene encoding the major outer membrane porin protein (MOMP) of Chlamydia trachomatis serovar L1 were ligated into the pUC plasmid vectors to give a series of overlapping recombinant sex pressing MOMP from the lac promoter. Induction of this promoter with IPTG leads to high‐level expression of the recombinant porin protein. Electron microscopy shows the presence of insoluble inclusions within the Escherichia coli host cells. Probing the expressed MOMP fragments with a set of monoclonal antibodies permitted localization of the four binding sites (epitopes)of primary‐sequence‐dependent monoclonal antibodies that exhibit genus‐, species‐, subspecies and type (serovar)‐specific reactivities.