Fig. 5. Proposed model for the mechanism of fluorescence reduction due to band 3 aggregation in AA and CC erythrocytes. Anti-band 3 mAb against cdb3 has easy access to band 3 epitopes in uninfected AA erythrocytes. During the course of P. falciparum infection, however, hemichromes form and bind with high affinity to the cdb3, hindering the anti-band 3 mAb binding. Band 3 also clusters to form oligomeric forms which may provide better recognition site for autologous antibody. Uninfected CC erythrocytes have increased band 3 oligomerization compared to uninfected AA erythrocytes, and a considerable amount of hemichromes already bound to the cdb3 that make those epitopes less accessible to anti-band 3 mAb, as shown in Fig. 1B. When these CC erythrocytes become infected, hemichromes form even larger deposits that further reduce antibody accessibility to band 3 epitopes, and band 3 forms higher levels of clustering, as shown Fig. 1A, Fig. 3B, Fig. 4E and 4F.