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• W2100048241 abstract "ABSTRACT EBA-175 of Plasmodium falciparum is a merozoite ligand that binds its receptor glycophorin A on erythrocytes during invasion. The ligand-receptor interaction is dependent on sialic acids as well as the protein backbone of glycophorin A. Region II (RII) of EBA-175 has been defined as the receptor-binding domain. RII is divided into regions F1 and F2, which contain duplicated cysteine motifs. We expressed RII in a baculovirus and show that RII binds erythrocytes with a specificity identical to that of the native protein. We found that, consistent with the binding of erythrocytes to COS cells expressing F2, recombinant baculovirus-expressed F2 bound erythrocytes. About 20% of all baculovirus-expressed RII is N-glycosylated, unlike native P. falciparum proteins that remain essentially unglycosylated. However, glycosylation of recombinant RII did not affect its immunogenicity. Antibodies raised against both glycosylated and unglycosylated baculovirus-expressed RII recognized P. falciparum schizonts in immunofluorescence assays and also gave similar enzyme-linked immunosorbent assay titers. Furthermore, these antibodies have similar abilities to block native EBA-175 binding to erythrocytes. These results allow the development of RII as a vaccine candidate for preclinical assessment." @default.
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• W2100048241 date "2000-06-01" @default.
• W2100048241 modified "2023-10-16" @default.
• W2100048241 title "A Recombinant Baculovirus-Expressed <i>Plasmodium falciparum</i> Receptor-Binding Domain of Erythrocyte Binding Protein EBA-175 Biologically Mimics Native Protein" @default.
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• W2100048241 doi "https://doi.org/10.1128/iai.68.6.3564-3568.2000" @default.
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