Frenkel Dan, Dori Mally, Solomon Beka
Department of Molecular Microbiology & Biotechnology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, Tel-Aviv 69978, Israel.
Vaccine. 2004 Jun 23;22(19):2505-8. doi: 10.1016/j.vaccine.2003.11.075.
The EFRH sequence, found to be the main anti-aggregating epitope corresponding to amino acids 3-6 of beta-amyloid peptide (AbetaP), was displayed on a phage and used as an antigen for immunization of mice, guinea pigs and rabbits. The generated antibodies recognize the full-length AbetaP (1-40) and exhibit similar biological properties to antibodies raised against whole soluble peptide and/or fibrillar beta-amyloid. EFRH-phage immunization of a transgenic mouse model of Alzheimer's disease evokes antibodies able to dissolve already formed beta-amyloid plaques, suggesting that they could become a therapeutic approach in treatment of the disease.
EFRH序列被发现是与β-淀粉样肽(AbetaP)的氨基酸3-6相对应的主要抗聚集表位,它被展示在噬菌体上,并用作免疫小鼠、豚鼠和兔子的抗原。所产生的抗体识别全长AbetaP(1-40),并表现出与针对全可溶性肽和/或纤维状β-淀粉样蛋白产生的抗体相似的生物学特性。对阿尔茨海默病转基因小鼠模型进行EFRH噬菌体免疫可诱发能够溶解已形成的β-淀粉样斑块的抗体,这表明它们可能成为治疗该疾病的一种治疗方法。