Zebedee S L, Barbas C F, Hom Y L, Caothien R H, Graff R, DeGraw J, Pyati J, LaPolla R, Burton D R, Lerner R A
R. W. Johnson Pharmaceutical Research Institute, San Diego, CA 92121.
Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3175-9. doi: 10.1073/pnas.89.8.3175.
Human antibody Fab fragments that bind to hepatitis B surface antigen (HBsAg) were generated by using a recombinant phage surface-display expression system. Characterization of HBsAg-specific Fab fragments isolated from two vaccinated individuals reveals diversity in specificity of antigen binding and in the sequences of the complementarity-determining region. The sequence results show examples of human light-chain promiscuity that result in fine specificity changes and a strong relationship to a human germ-line gene. This application illustrates further that this technique is a powerful tool to isolate distinct human antibodies against immunogenic viral targets.
利用重组噬菌体表面展示表达系统产生了与乙型肝炎表面抗原（HBsAg）结合的人源抗体Fab片段。对从两名接种疫苗个体中分离出的HBsAg特异性Fab片段进行的表征揭示了抗原结合特异性和互补决定区序列的多样性。序列结果显示了人轻链混杂的例子，这些例子导致了精细的特异性变化以及与人类种系基因的强相关性。该应用进一步表明，这项技术是分离针对免疫原性病毒靶点的独特人源抗体的有力工具。
