Identification, cloning, and purification of protein antigens of Treponema pallidum.
Difficulties in culturing the bacterium Treponema pallidum have greatly hindered syphilis research. In recent years, several laboratories have begun applying recombinant DNA technology to the study of this organism. Recent work is summarized concerning the expression of T. pallidum DNA in Escherichia coli. A number of E. coli clones expressing treponemal protein antigens have been identified. In one instance, a recombinant protein was purified to homogeneity and shown to be identical to a highly immunogenic, native T. pallidum membrane protein of molecular weight 39,000, which was designated the basic membrane protein (BMP) of this organism. In addition, recent experiments are described that were designed to identify cell-surface proteins that would serve as the primary focus of our cloning efforts. Results obtained with use of several different approaches strongly suggest that the outer membrane of T. pallidum is an antigenically inert structure largely devoid of protein. However, a class of low-molecular-weight protein antigens have been identified that are actively secreted into the extracellular medium. Attempts currently are being made to clone these secreted proteins and investigate their roles in the pathogenesis and immunobiology of syphilis.
Stamm
L V
LV
Department of Parasitology and Laboratory Practice, School of Public Health, University of North Carolina, Chapel Hill 27514.
Dallas
W S
WS
Ray
P H
PH
Bassford
P J
PJ
D000818:Animals; D000942:Antigens, Bacterial / Q000235:genetics* / Q000302:isolation & purification; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification; D014210:Treponema pallidum / Q000235:genetics / Q000276:immunology*
D000942:Antigens, Bacterial; D011994:Recombinant Proteins