Band 3 clustering promotes the exposure of neoantigens in Plasmodium falciparum-infected erythrocytes

• Published in: Molecular and biochemical parasitology 2005-07, Vol.142 (1), p.98-105
• Main Authors: Winograd, Enrique, Prudhomme, Jacques G., Sherman, Irwin W.
• Format: Article
• Language: English
• Subjects: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid - metabolism; Amino Acid Sequence; Animals; Anion Exchange Protein 1, Erythrocyte - chemistry; Anion Exchange Protein 1, Erythrocyte - genetics; Anion Exchange Protein 1, Erythrocyte - immunology; Anion Exchange Protein 1, Erythrocyte - metabolism; Antibodies, Protozoan - immunology; Antigens, Protozoan - chemistry; Antigens, Protozoan - immunology; Antigens, Protozoan - metabolism; Band 3; Cell Adhesion; DIDS binding region; Erythrocyte Membrane - chemistry; Erythrocyte Membrane - immunology; Erythrocytes - parasitology; Erythrocytes - physiology; Humans; Malaria; Malaria, Falciparum - immunology; Malaria, Falciparum - parasitology; Mice; Plasmodium falciparum; Plasmodium falciparum - immunology; Plasmodium falciparum - pathogenicity; Rabbits
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/j.molbiopara.2005.03.013

Erythrocytes infected with the human malaria parasite Plasmodium falciparum become structurally and antigenically modified as a consequence of intracellular parasite development. The new antigens that appear on the surface of the infected erythrocyte originate from parasite-encoded proteins and by modification of the erythrocyte membrane protein band 3. Here, we show that anti-peptide antibodies generated against an amino acid sequence (YETFSKLIKIFQDH) of human band 3, and previously identified as mediating adhesion of infected erythrocytes to CD36, recognized P. falciparum-infected erythrocytes. In addition, sera from individuals living in a malaria endemic area (and who are presumably immune) contained immunoglobulins specific for this region of band 3. The anti-peptide antibodies reacted with the surface excrescences (knobs) on falciparum-infected erythrocytes. In uninfected erythrocytes, the band 3 region was cryptic and its exposure on the falciparum-infected erythrocyte surface required clustering of band 3 protein. Thus, a parasite-induced modification of band 3 promotes adhesion and induces antigenic changes in the P. falciparum-infected erythrocyte.