Fischer P M, Howden M E
Department of Biological Sciences, Deakin University, Geelong, Victoria, Australia.
Mol Immunol. 1994 Oct;31(15):1141-8. doi: 10.1016/0161-5890(94)90028-0.
In this study the immunochemical structure of the heavy chain polypeptide from tetanus toxin was studied. Numerous antigenic determinants were identified by probing a set of overlapping peptides derived from the amino acid sequence of tetanus toxin with polyclonal anti-toxoid antibody preparations. Synthetic antigens representing continuous epitopes were prepared and used to immunize mice. The capacity of the resulting anti-peptide antibodies to react with tetanus toxin in vitro and in vivo was determined. The majority of antibodies bound to tetanus toxin and three epitopes capable of eliciting neutralizing antibodies were identified.
在本研究中,对破伤风毒素重链多肽的免疫化学结构进行了研究。通过用多克隆抗类毒素抗体制剂探测一组源自破伤风毒素氨基酸序列的重叠肽,鉴定出了许多抗原决定簇。制备了代表连续表位的合成抗原,并用于免疫小鼠。测定了所得抗肽抗体在体外和体内与破伤风毒素反应的能力。大多数抗体与破伤风毒素结合,并鉴定出了三个能够引发中和抗体的表位。