| Syphilis is a chronic, complex, systemic sexually transmitted disease of humans over the world caused by the bacteria Treponema pallidum subsp. pallidum (T. pallidum). Because T. pallidum cannot be readily cultured in vitro, For most research and diagnostic purposes the pathogenic strain Nichols are passaged and propagated by serial intratesticular infection of rabbits. Disadvantages of this method are high cost, only limited quantities of bacteria, however, can be obtained. Also, T. pallidum isolated from tissue characteristically is contaminated with host tissue components, regardless of the bacterial isolation strategy used as well as the difficulties in purifying of specific polypeptides because of the complexity of T. pallidum antigenic structures. Furthermore, isolation and purification processes compromise the structural integrity of the fragile organisms. These limitations have restricted progress in elucidating the morphology, structure, physiology, and genetics of T. pallidum. Perhaps most importantly, they have hampered the identification of molecular components of the organism that may influence pathogenesis and the immune response of the host during syphilitic infection. It has not been feasible to directly assess the biological importance of individual antigens of T. pallidum. Despite of these obstacles, a group of highly antigenic, T. pallidum-specific membrane proteins were isolated by phase partitioning with the nonionic detergent Triton-114. Included among these membrane immunogens were the 47-, 17-, and 15-kilodalton (kD) lipoprotein. Since then there are many experiments have supported the results. In this report, we prepared three recombinant lipoprotein antigens designated rTpp47, rTpp17, and rTpp15 by genetic engineering technique, and analyzed preliminarily on the reactivity of rTpp47 and rTpp17 with...
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