Identification and characterization of peptide mimics of blood group A antigen

作者：Tang Zhaoming; Wang Lin; Hu Lihua^*; Li Yirong; Cui Tianpen; Xiong Juan; Dou Lifang

来源：Journal of Huazhong University of Science and Technology-Medical Sciences, 2008, 28(2): 222-226.

DOI：10.1007/s11596-008-0228-0

• amino acid sequence
• blood group A antigen
• hemagglutination test
• molecular mimicry
• peptide library

In order to investigate peptide mimics of carbohydrate blood group A antigen, a phage display 12-mer peptide library was screened with a monoclonal antibody against blood group A antigen, NaM87-1F6. The antibody-binding properties of the selected phage peptides were evaluated by phage ELISA and phage capture assay. The peptides were co-expressed as glutathione S-transferase (GST) fusion proteins. RBC agglutination inhibition assay was performed to assess the natural blood group A antigen-mimicking ability of the fusion proteins. The results showed that seven phage clones selected bound to NaM87-1F6 specifically, among which, 6 clones bore the same peptide sequence, EYWYCGMNRTGC and another harbored a different one QIWYERTLPFTF. The two peptides were successfully expressed at the N terminal of GST protein. Both of the fusion proteins inhibited the RBC agglutination mediated by anti-A serum in a concentration-dependent manner. These results suggested that the fusion proteins based on the selected peptides could mimic the blood group A antigen and might be used as anti-A antibody-adsorbing materials when immunoabsorption was applied in ABO incompatible transplantation.

• 出版日期2008-4
• 单位华中科技大学