Christiansen G, Mathiesen S L, Nyvold C, Birkelund S
Institute of Medical Microbiology, University of Aarhus, Denmark.
FEMS Microbiol Lett. 1994 Aug 1;121(1):121-7. doi: 10.1111/j.1574-6968.1994.tb07085.x.
The monoclonal antibody mAb 26.7D generated against a clinical isolate of Mycoplasma hominis 7488 was shown to react with a surface-exposed epitope on a 120-kDa protein (P120). The gene encoding the protein was cloned and sequenced, and the transcriptional start point was determined by primer extension analysis. The gene contained an open reading frame of 3237 bp encoding a peptide of 1079 amino acids with a deduced molecular mass of 123 kDa. A putative amino-terminal signal peptide and cleavage site for signal peptidase II were found. This suggests that the protein was synthesized as a precursor with subsequent processing to a mature lipoprotein. Surface exposure was confirmed by immunoelectron microscopy. mAb 26.7D reacted with 11 of 19 M. hominis strains. The gene was, however, present in all strains.
针对人型支原体7488临床分离株产生的单克隆抗体mAb 26.7D被证明可与120 kDa蛋白（P120）上的一个表面暴露表位发生反应。编码该蛋白的基因被克隆并测序，转录起始点通过引物延伸分析确定。该基因包含一个3237 bp的开放阅读框，编码一个1079个氨基酸的肽段，推导分子量为123 kDa。发现了一个假定的氨基末端信号肽和信号肽酶II的切割位点。这表明该蛋白以前体形式合成，随后加工成成熟的脂蛋白。免疫电子显微镜证实了其表面暴露。mAb 26.7D与19株人型支原体中的11株发生反应。然而，该基因存在于所有菌株中。
