Species-Specific Epitopes Exist on the Cytoplasmic Amino-Terminal Domain of Erythrocyte Band 3 Protein1

Abstract

Monoclonal antibodies (P3-9H, P3-1F, P3-2H, P3-4A, and P3-4C) to human erythrocyte band 3 were produced using human erythrocyte membranes as the immunogen. All epitopes defined by these antibodies were found on the amino-terminal cytoplasmic domain of erythrocyte band 3. The antibodies crossreacted variously with erythrocyte band 3 of primates (chimpanzee, orangutan, Rhesus monkey, Japanese monkey, spider monkey, and capuchin monkey) in enzyme-linked immunosorbent assay. P3-9H did not crossreact with erythrocyte band 3 of any primate examined; P3-1F crossreacted only with that of chimpanzee; P3-2H crossreacted with erythrocyte band 3 of chimpanzee, spider monkey, and capuchin monkey; and P3-4A and P3-4C crossreacted with erythrocyte band 3 of all primates examined. These results suggest that evolutional changes in primates are accumulated in the amino-terminal cytoplasmic domain of band 3 and that species-specific epitopes exist on this domain.

Identification of a cross‐reacting, monoclonal anti‐human CD233 antibody for identification and sorting of rhesus macaque erythrocytes

“…It associates the plasma membrane with the red cell cytoskeleton by binding ankyrin, thereby helping to maintain cellular structure and stability (17, 18). High level binding of anti-CD233 is due to its abundance on the cell surface (approximately 25% of the plasma membrane protein) (19).…”