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.
Artículo
en Inglés
| 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.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Péptidos
/
Bacteriófagos
/
Antígenos de Grupos Sanguíneos
/
Proteínas Recombinantes de Fusión
/
Ensayo de Inmunoadsorción Enzimática
/
Estructura Terciaria de Proteína
/
Adsorción
/
Biblioteca de Péptidos
/
Glutatión Transferasa
/
Epítopos
Tipo de estudio:
Estudio diagnóstico
Idioma:
Inglés
Revista:
Journal of Huazhong University of Science and Technology (Medical Sciences)
Año:
2008
Tipo del documento:
Artículo
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