Conlan J W, Ferris S, Clarke I N, Ward M E
Department of Microbiology, University of Southampton Medical School, UK.
J Gen Microbiol. 1990 Oct;136(10):2013-20. doi: 10.1099/00221287-136-10-2013.
Recombinant fragments of the major outer-membrane protein (MOMP) of Chlamydia trachomatis, expressed at high levels in Escherichia coli, were isolated and purified. Antisera to the recombinant proteins reacted preferentially with overlapping synthetic peptides covering the immunoaccessible variable segments of MOMP. These sera also reacted in a species-specific manner with the surface of intact infectious elementary bodies, and in a Chlamydia genus-specific manner in assays using denatured or bound chlamydial antigens. The ability of recombinant MOMP preparations to elicit antibody to the surface of chlamydial elementary bodies raises the possibility that these proteins may be useful for chlamydial vaccine development.
沙眼衣原体主要外膜蛋白(MOMP)的重组片段在大肠杆菌中高水平表达,经分离和纯化后,针对这些重组蛋白的抗血清优先与覆盖MOMP免疫可及可变区的重叠合成肽发生反应。这些血清还以种属特异性方式与完整感染性原体的表面发生反应,并在使用变性或结合衣原体抗原的检测中以衣原体属特异性方式发生反应。重组MOMP制剂引发针对衣原体原体表面抗体的能力增加了这些蛋白质可能对衣原体疫苗开发有用的可能性。