Identification and Characterization of Peptide Mimics of Blood Group A Antigen
- Author:
TANG ZHAOMING
1
;
WANG LIN
;
HU LIHUA
;
LI YIRONG
;
CUI TIANPEN
;
XIONG JUAN
;
DOU LIFANG
Author Information
1. 华中科技大学同济医学院附属协和医院
- Keywords:
amino acid sequence;
blood group A antigen;
hemagglutination test;
molecular mimicry;
peptide library
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2008;28(2):222-226
- CountryChina
- Language:Chinese
-
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.
