Expression of the chlamydial genus-specific lipopolysaccharide epitope in Escherichia coli.
The obligate intracellular prokaryote Chlamydia trachomatis is the etiological agent of trachoma and is a primary causative pathogen of sexually transmitted genital tract disease; both diseases affect millions of people each year. The cloning of genes encoding the enzyme or enzymes producing the genus-specific lipopolysaccharide antigen of Chlamydia into Escherichia coli is reported here. The cloned chlamydial lipopolysaccharide antigen appears to be a hybrid lipopolysaccharide molecule composed of both Chlamydia and Escherichia coli components. The chlamydial lipopolysaccharide antigen is expressed on the surfaces of the viable Escherichia coli recombinants. These findings may have a significant impact on defining the role of this highly conserved antigen in the pathogenesis and diagnosis of chlamydial infections.
Nano
F E
FE
Caldwell
H D
HD
D002690:Chlamydia Infections / Q000276:immunology; D002692:Chlamydia trachomatis / Q000235:genetics* / Q000276:immunology; D004274:DNA, Recombinant / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D005455:Fluorescent Antibody Technique; D005818:Genetic Engineering; D006367:HeLa Cells / Q000382:microbiology; D008070:Lipopolysaccharides / Q000235:genetics* / Q000276:immunology
D004274:DNA, Recombinant; D000939:Epitopes; D008070:Lipopolysaccharides