Glycophorin A is recognized by an antibody population of the rabbit polyclonal antibodies produced against Citrobacter braakii O37.

摘要: Background and Purpose: Molecular mimicry was found in the case of Citrobacter braakii O37, which shares epitopes with human erythrocytes. It is believed that erythrocyte-membrane proteins band 3 glycophorin A (GPA) have common epitopes. Band recognized by anti-C. O37 lipopolysaccharide antibodies (LPS-Abs) purified on LPS-affinity columns. This study aimed to investigate role GPA this molecular mimicry. Methods: Immunochemical methods such as immunoblotting, enzyme-linked immunosorbent assay, inhibition hemagglutination, affinity columns were employed. Results: when immobilized an column could purify specific (GPA-Abs) from whole serum. The antibodies, turn, immunoblotting tests. Treatment erythrocytes sialidase significantly improved hemagglutination titer GPA-Abs. Furthermore, inhibited a greater extent asialo-GPA than native form. blood groups M N similarly inhibit most significant recorded group MN. GPA-Abs not recognize LPS C. O37. Conclusions: Results confirmed antibody population serum GPA. However, there no reactivity indicating may be produced against outer membrane protein bacteria.