Receptor binding domain of glycophorin A for Plasmodium falciparum surface proteins
Davidson, E.A.; Perkins, M.E.
Indian Journal of Biochemistry and Biophysics 25(1-2): 90-94
1988
ISSN/ISBN: 0301-1208 PMID: 3053416 Document Number: 309244
Plasmodium falciparum merozoites interact with the erythrocyte sialoglycoproteins glycophorin A and B during invasion into the host cell. Two P. falciparum roteins binding to glycophorin A and B were identified in 6 different geographic isolates of the parasite. The binding of the parasite proteins to a glycophorin-acrylamide affinity matrix was inhibited by the N-terminal tryptic peptide of glycophorin A (amino acids 1-39) but not by the other tryptic peptides (T3-T6) spanning the remainder of this transmembrane protein. Binding was also inhibited by the CNBr fragment of the T1 peptide (amino acids 8-39). The T1 tryptic peptide coupled to acrylamide possessed the full binding activity of intact glycophorin. Desialylation of the T1 peptide resulted in loss of ability of the fragment of competitively inhibit binding of the parasite glycophorin binding proteins. This suggests that the terminal NeuNac residues of the oligosaccharide chains are essential features of the parasite protein binding site specified by the N-terminal domain of glycophorin A.