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): 222-6, 2008.
Article
in English
| WPRIM
| ID: wpr-634651
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Peptides
/
Bacteriophages
/
Blood Group Antigens
/
Recombinant Fusion Proteins
/
Enzyme-Linked Immunosorbent Assay
/
Protein Structure, Tertiary
/
Adsorption
/
Peptide Library
/
Glutathione Transferase
/
Epitopes
Type of study:
Diagnostic study
Language:
English
Journal:
Journal of Huazhong University of Science and Technology (Medical Sciences)
Year:
2008
Type:
Article
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