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Identification and Characterization of Peptide Mimics of Blood Group A Antigen / 华中科技大学学报(医学)(英德文版)
Journal of Huazhong University of Science and Technology (Medical Sciences) ; (6): 222-226, 2008.
Article in Chinese | WPRIM | ID: wpr-284602
ABSTRACT
In order to investigate peptide mimics of carbohydrate blood group A antigen, a phage display 12-met 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 QIWYERTLPFrF. 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 an- tigen and might be used as anti-A antibody-adsorbing materials when immunoabsorption was applied in ABO incompatible transplantation.

Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Journal of Huazhong University of Science and Technology (Medical Sciences) Year: 2008 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Journal of Huazhong University of Science and Technology (Medical Sciences) Year: 2008 Type: Article