Identification and characterization of peptide mimics of blood group A antigen.
- Author:
Zhaoming, TANG
;
Lin, WANG
;
Lihua, HU
;
Yirong, LI
;
Tianpen, CUI
;
Juan, XIONG
;
Lifang, DOU
- Publication Type:Journal Article
- MeSH:
Adsorption;
Bacteriophages;
Blood Group Antigens/*chemistry;
Enzyme-Linked Immunosorbent Assay;
Epitopes/chemistry;
Glutathione Transferase/metabolism;
Peptide Library;
Peptides/*chemistry;
Protein Structure, Tertiary;
Recombinant Fusion Proteins/chemistry
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2008;28(2):222-6
- CountryChina
- Language:English
-
Abstract:
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.
